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- PDB-8woe: Cryo-EM structure of the intact flagellar motor-hook complex in t... -

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Basic information

Entry
Database: PDB / ID: 8woe
TitleCryo-EM structure of the intact flagellar motor-hook complex in the CW state
Components
  • (Flagellar basal-body rod protein ...) x 3
  • (Flagellar biosynthetic protein ...) x 3
  • (Flagellar motor switch protein ...) x 3
  • Chemotaxis protein CheY
  • Flagellar L-ring protein
  • Flagellar M-ring protein
  • Flagellar P-ring protein
  • Flagellar basal body rod protein FlgB
  • Flagellar hook protein FlgE
  • Flagellar hook-basal body complex protein FliE
KeywordsMOTOR PROTEIN / Flagellum / Flagellar motor / C ring / Switch complex / CheY
Function / homology
Function and homology information


bacterial-type flagellum basal body, distal rod, L ring / bacterial-type flagellum basal body, distal rod, P ring / bacterial-type flagellum basal body, distal rod / bacterial-type flagellum basal body, rod / bacterial-type flagellum organization / bacterial-type flagellum hook / archaeal or bacterial-type flagellum-dependent cell motility / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility ...bacterial-type flagellum basal body, distal rod, L ring / bacterial-type flagellum basal body, distal rod, P ring / bacterial-type flagellum basal body, distal rod / bacterial-type flagellum basal body, rod / bacterial-type flagellum organization / bacterial-type flagellum hook / archaeal or bacterial-type flagellum-dependent cell motility / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / bacterial-type flagellum / positive chemotaxis / phosphorelay signal transduction system / bacterial-type flagellum assembly / cytoskeletal motor activity / protein secretion / bacterial-type flagellum-dependent cell motility / protein targeting / cell outer membrane / chemotaxis / outer membrane-bounded periplasmic space / structural molecule activity / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Flagellar L-ring protein / Flagellar L-ring protein / Flagellar P-ring protein / Flagellar P-ring protein / Flagellar basal-body rod protein FlgC / Flagellar basal-body rod FlgG / Flagellar hook-basal body complex protein FliE / Flagellar basal-body rod protein FlgB / Flagellar hook-basal body complex protein FliE / Flagellar motor switch protein FliN, N-terminal ...Flagellar L-ring protein / Flagellar L-ring protein / Flagellar P-ring protein / Flagellar P-ring protein / Flagellar basal-body rod protein FlgC / Flagellar basal-body rod FlgG / Flagellar hook-basal body complex protein FliE / Flagellar basal-body rod protein FlgB / Flagellar hook-basal body complex protein FliE / Flagellar motor switch protein FliN, N-terminal / Flagellar motor switch protein FliN N-terminal / Flagellar biosynthesis protein FliQ / : / Flagellar biosynthesis protein FliR / Flagellar motor switch FliN / Flagellar motor switch FliN/Type III secretion HrcQb / Flagellar transport protein FliP / Flagellar motor switch protein FliM / Flagellar hook protein FlgE superfamily / Flagellar motor switch protein FliM / Flagellar hook protein FlgE / Flagellar basal body protein FlaE D2 domain / Flagellar motor switch protein FliG / Flagellar motor switch protein FliG, alpha-helical / Flagellar motor switch protein FliG, C-terminal / Flagellar motor switch protein FliG, N-terminal domain / Flagellar motor switch protein FliG, middle domain / FliG C-terminal domain / FliG middle domain / FliG N-terminal domain / Type III secretion system inner membrane R protein / Bacterial export protein family 3 / Flagellar hook-basal body protein, FlgE/F/G / CheC-like superfamily / Flagellar hook-basal body protein, FlgE/F/G-like / : / Bacterial export proteins, family 1 / Bacterial export proteins, family 3 / Flagellar hook protein FlgE/F/G D1 domain / Flagella transport protein fliP family signature 1. / Flagellar motor switch protein FliN-like, C-terminal domain / Type III secretion system inner membrane P protein / SpoA-like superfamily / FliP family / Type III flagellar switch regulator (C-ring) FliN C-term / Flagella transport protein fliP family signature 2. / Flagellar basal body rod protein, conserved site / Flagella basal body rod proteins signature. / Flagellar basal body rod protein, N-terminal / Flagellar basal-body/hook protein, C-terminal domain / Flagella basal body rod protein / Flagellar basal body rod FlgEFG protein C-terminal / : / Flagellar M-ring protein FliF / Flagellar M-ring C-terminal / Flagellar M-ring protein C-terminal / Lipoprotein YscJ/Flagellar M-ring protein / Secretory protein of YscJ/FliF family / Flagellar M-ring , N-terminal / AMP-binding enzyme, C-terminal domain superfamily / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
Flagellar basal-body rod protein FlgC / Flagellar hook protein FlgE / Flagellar basal-body rod protein FlgG / Flagellar motor switch protein FliG / Flagellar biosynthetic protein FliQ / Flagellar L-ring protein / Chemotaxis protein CheY / Flagellar M-ring protein / Flagellar P-ring protein / Flagellar basal-body rod protein FlgF ...Flagellar basal-body rod protein FlgC / Flagellar hook protein FlgE / Flagellar basal-body rod protein FlgG / Flagellar motor switch protein FliG / Flagellar biosynthetic protein FliQ / Flagellar L-ring protein / Chemotaxis protein CheY / Flagellar M-ring protein / Flagellar P-ring protein / Flagellar basal-body rod protein FlgF / Flagellar basal body rod protein FlgB / Flagellar motor switch protein FliM / Flagellar motor switch protein FliN / Flagellar hook-basal body complex protein FliE / Flagellar biosynthetic protein FliP / Flagellar biosynthetic protein FliR
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å
AuthorsTan, J.X. / Zhang, L. / Zhou, Y. / Zhu, Y.Q.
Funding support China, 3items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)81925024 China
National Natural Science Foundation of China (NSFC)U23A20163 China
Ministry of Science and Technology (MoST, China)2017YFA0503900 China
CitationJournal: Cell Res / Year: 2024
Title: Structural basis of the bacterial flagellar motor rotational switching.
Authors: Jiaxing Tan / Ling Zhang / Xingtong Zhou / Siyu Han / Yan Zhou / Yongqun Zhu /
Abstract: The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the ...The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive. Here, we present two high-resolution cryo-electron microscopy structures of the C ring-containing flagellar basal body-hook complex from Salmonella Typhimurium, which are in the default counterclockwise state and in a constitutively active CheY mutant-induced clockwise state, respectively. In both complexes, the C ring consists of four subrings, but is in two different conformations. The CheY proteins are bound into an open groove between two adjacent protomers on the surface of the middle subring of the C ring and interact with the FliG and FliM subunits. The binding of the CheY protein induces a significant upward shift of the C ring towards the MS ring and inward movements of its protomers towards the motor center, which eventually remodels the structures of the FliG subunits and reverses the orientations and surface electrostatic potential of the α helices to trigger the counterclockwise-to-clockwise rotational switching. The conformational changes of the FliG subunits reveal that the stator units on the motor require a relocation process in the inner membrane during the rotational switching. This study provides unprecedented molecular insights into the rotational switching mechanism and a detailed overall structural view of the bacterial flagellar motors.
History
DepositionOct 7, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 4, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 30, 2024Group: Data collection / Structure summary
Category: em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.last_update
Revision 1.2Mar 26, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: Flagellar basal-body rod protein FlgG
1: Flagellar basal-body rod protein FlgG
2: Flagellar basal-body rod protein FlgG
3: Flagellar basal-body rod protein FlgG
4: Flagellar basal-body rod protein FlgG
5: Flagellar basal-body rod protein FlgG
6: Flagellar basal-body rod protein FlgG
7: Flagellar basal-body rod protein FlgG
8: Flagellar basal-body rod protein FlgG
9: Flagellar basal-body rod protein FlgG
A: Flagellar L-ring protein
A0: Flagellar basal body rod protein FlgB
A1: Flagellar hook-basal body complex protein FliE
A2: Flagellar hook-basal body complex protein FliE
A3: Flagellar hook-basal body complex protein FliE
A4: Flagellar hook-basal body complex protein FliE
A5: Flagellar hook-basal body complex protein FliE
A6: Flagellar basal body rod protein FlgB
A7: Flagellar basal body rod protein FlgB
A8: Flagellar basal body rod protein FlgB
A9: Flagellar basal body rod protein FlgB
AA: Flagellar basal-body rod protein FlgF
AB: Flagellar basal-body rod protein FlgF
AC: Flagellar basal-body rod protein FlgF
AD: Flagellar basal-body rod protein FlgF
AE: Flagellar basal-body rod protein FlgF
AF: Flagellar basal-body rod protein FlgG
AG: Flagellar basal-body rod protein FlgG
AH: Flagellar basal-body rod protein FlgG
AI: Flagellar basal-body rod protein FlgG
AJ: Flagellar basal-body rod protein FlgG
AK: Flagellar basal-body rod protein FlgG
AL: Flagellar basal-body rod protein FlgG
AM: Flagellar basal-body rod protein FlgG
AN: Flagellar basal-body rod protein FlgG
AO: Flagellar M-ring protein
AP: Flagellar M-ring protein
AQ: Flagellar M-ring protein
AR: Flagellar M-ring protein
AS: Flagellar M-ring protein
AT: Flagellar M-ring protein
AU: Flagellar M-ring protein
AV: Flagellar M-ring protein
AW: Flagellar M-ring protein
AX: Flagellar M-ring protein
AY: Flagellar M-ring protein
AZ: Flagellar M-ring protein
Aa: Flagellar M-ring protein
Ab: Flagellar biosynthetic protein FliQ
Ac: Flagellar M-ring protein
Ad: Flagellar M-ring protein
Ae: Flagellar M-ring protein
Af: Flagellar M-ring protein
Ag: Flagellar M-ring protein
Ah: Flagellar M-ring protein
Ai: Flagellar M-ring protein
Aj: Flagellar M-ring protein
Ak: Flagellar M-ring protein
Al: Flagellar M-ring protein
Am: Flagellar M-ring protein
An: Flagellar M-ring protein
Ao: Flagellar M-ring protein
Ap: Flagellar M-ring protein
Aq: Flagellar biosynthetic protein FliQ
Ar: Flagellar biosynthetic protein FliQ
As: Flagellar biosynthetic protein FliQ
At: Flagellar biosynthetic protein FliR
Au: Flagellar biosynthetic protein FliP
Av: Flagellar biosynthetic protein FliP
Aw: Flagellar biosynthetic protein FliP
Ax: Flagellar biosynthetic protein FliP
Ay: Flagellar biosynthetic protein FliP
Az: Flagellar hook-basal body complex protein FliE
B: Flagellar L-ring protein
BA: Flagellar basal-body rod protein FlgC
BB: Flagellar basal-body rod protein FlgC
BC: Flagellar basal-body rod protein FlgC
BD: Flagellar basal-body rod protein FlgC
BE: Flagellar basal-body rod protein FlgC
BF: Flagellar basal-body rod protein FlgC
BG: Flagellar M-ring protein
BH: Flagellar M-ring protein
BI: Flagellar M-ring protein
BJ: Flagellar M-ring protein
BK: Flagellar M-ring protein
BL: Flagellar M-ring protein
BM: Flagellar M-ring protein
BN: Flagellar M-ring protein
BO: Flagellar M-ring protein
BP: Flagellar M-ring protein
BQ: Flagellar M-ring protein
BR: Flagellar M-ring protein
BS: Flagellar M-ring protein
BT: Flagellar M-ring protein
BU: Flagellar M-ring protein
BV: Flagellar M-ring protein
BW: Flagellar M-ring protein
BX: Flagellar M-ring protein
C: Flagellar L-ring protein
D: Flagellar L-ring protein
E: Flagellar L-ring protein
F: Flagellar L-ring protein
G: Flagellar L-ring protein
H: Flagellar L-ring protein
I: Flagellar L-ring protein
J: Flagellar L-ring protein
K: Flagellar L-ring protein
L: Flagellar L-ring protein
M: Flagellar L-ring protein
N: Flagellar L-ring protein
O: Flagellar L-ring protein
P: Flagellar L-ring protein
Q: Flagellar L-ring protein
R: Flagellar L-ring protein
S: Flagellar L-ring protein
T: Flagellar L-ring protein
U: Flagellar L-ring protein
UI: Flagellar M-ring protein
UJ: Flagellar M-ring protein
UK: Flagellar M-ring protein
UL: Flagellar M-ring protein
UM: Flagellar M-ring protein
UN: Flagellar M-ring protein
UO: Flagellar M-ring protein
UP: Flagellar M-ring protein
V: Flagellar L-ring protein
W: Flagellar L-ring protein
WA: Flagellar M-ring protein
WB: Flagellar M-ring protein
WC: Flagellar M-ring protein
WD: Flagellar M-ring protein
WE: Flagellar M-ring protein
WF: Flagellar M-ring protein
WG: Flagellar M-ring protein
WH: Flagellar M-ring protein
WI: Flagellar M-ring protein
WJ: Flagellar M-ring protein
WK: Flagellar M-ring protein
WL: Flagellar M-ring protein
WM: Flagellar M-ring protein
WN: Flagellar M-ring protein
WO: Flagellar M-ring protein
WP: Flagellar M-ring protein
WQ: Flagellar M-ring protein
WR: Flagellar M-ring protein
WS: Flagellar M-ring protein
WT: Flagellar M-ring protein
WU: Flagellar M-ring protein
WV: Flagellar M-ring protein
WW: Flagellar M-ring protein
X: Flagellar L-ring protein
Y: Flagellar L-ring protein
Z: Flagellar L-ring protein
ZA: Flagellar basal-body rod protein FlgG
ZB: Flagellar basal-body rod protein FlgG
ZC: Flagellar basal-body rod protein FlgG
ZD: Flagellar basal-body rod protein FlgG
ZE: Flagellar basal-body rod protein FlgG
ZF: Flagellar hook protein FlgE
ZG: Flagellar hook protein FlgE
ZH: Flagellar hook protein FlgE
ZI: Flagellar hook protein FlgE
ZJ: Flagellar hook protein FlgE
ZK: Flagellar hook protein FlgE
ZL: Flagellar hook protein FlgE
ZM: Flagellar hook protein FlgE
ZN: Flagellar hook protein FlgE
ZO: Flagellar hook protein FlgE
ZP: Flagellar hook protein FlgE
ZQ: Flagellar hook protein FlgE
ZR: Flagellar hook protein FlgE
ZS: Flagellar hook protein FlgE
ZT: Flagellar hook protein FlgE
ZU: Flagellar hook protein FlgE
ZV: Flagellar hook protein FlgE
ZW: Flagellar hook protein FlgE
ZX: Flagellar hook protein FlgE
ZY: Flagellar hook protein FlgE
ZZ: Flagellar hook protein FlgE
Za: Flagellar hook protein FlgE
Zb: Flagellar hook protein FlgE
Zc: Flagellar hook protein FlgE
Zd: Flagellar hook protein FlgE
Ze: Flagellar hook protein FlgE
Zf: Flagellar hook protein FlgE
Zg: Flagellar hook protein FlgE
Zh: Flagellar hook protein FlgE
a: Flagellar P-ring protein
b: Flagellar P-ring protein
c: Flagellar P-ring protein
d: Flagellar P-ring protein
e: Flagellar P-ring protein
f: Flagellar P-ring protein
g: Flagellar P-ring protein
h: Flagellar P-ring protein
i: Flagellar P-ring protein
j: Flagellar P-ring protein
k: Flagellar P-ring protein
l: Flagellar P-ring protein
m: Flagellar P-ring protein
n: Flagellar P-ring protein
o: Flagellar P-ring protein
p: Flagellar P-ring protein
q: Flagellar P-ring protein
r: Flagellar P-ring protein
s: Flagellar P-ring protein
t: Flagellar P-ring protein
u: Flagellar P-ring protein
v: Flagellar P-ring protein
w: Flagellar P-ring protein
x: Flagellar P-ring protein
y: Flagellar P-ring protein
z: Flagellar P-ring protein
C3: Flagellar motor switch protein FliN
C4: Flagellar motor switch protein FliN
C5: Flagellar motor switch protein FliN
C6: Flagellar motor switch protein FliG
C7: Chemotaxis protein CheY
C8: Flagellar motor switch protein FliN
C9: Flagellar motor switch protein FliN
C0: Flagellar motor switch protein FliM
DA: Flagellar motor switch protein FliG
DB: Chemotaxis protein CheY
DC: Flagellar motor switch protein FliM
DD: Flagellar motor switch protein FliN
DE: Flagellar M-ring protein
DF: Flagellar motor switch protein FliM
DG: Flagellar motor switch protein FliG
DH: Chemotaxis protein CheY
DI: Flagellar motor switch protein FliN
DJ: Flagellar motor switch protein FliN
DK: Flagellar motor switch protein FliN
DL: Flagellar M-ring protein
DM: Flagellar motor switch protein FliN
DN: Flagellar motor switch protein FliN
DO: Flagellar motor switch protein FliN
DP: Flagellar motor switch protein FliN
DQ: Flagellar motor switch protein FliN
DR: Flagellar motor switch protein FliN
DS: Flagellar motor switch protein FliN
DT: Flagellar motor switch protein FliN
DU: Flagellar motor switch protein FliN
DV: Flagellar motor switch protein FliN
DW: Flagellar motor switch protein FliN
DX: Flagellar motor switch protein FliM
DY: Flagellar motor switch protein FliG
DZ: Chemotaxis protein CheY
Da: Flagellar motor switch protein FliN
Db: Flagellar motor switch protein FliN
Dc: Flagellar motor switch protein FliN
Dd: Flagellar motor switch protein FliM
De: Flagellar motor switch protein FliG
Df: Chemotaxis protein CheY
Dg: Flagellar motor switch protein FliN
Dh: Flagellar motor switch protein FliN
Di: Flagellar motor switch protein FliN
Dj: Flagellar motor switch protein FliM
Dk: Flagellar motor switch protein FliG
Dl: Chemotaxis protein CheY
Dm: Flagellar motor switch protein FliN
Dn: Flagellar motor switch protein FliN
Do: Flagellar motor switch protein FliN
Dp: Flagellar motor switch protein FliM
Dq: Flagellar motor switch protein FliG
Dr: Chemotaxis protein CheY
Ds: Flagellar motor switch protein FliN
Dt: Flagellar motor switch protein FliN
Du: Flagellar motor switch protein FliN
Dv: Flagellar motor switch protein FliM
Dw: Flagellar motor switch protein FliG
Dx: Chemotaxis protein CheY
Dy: Flagellar motor switch protein FliN
Dz: Flagellar motor switch protein FliN
D1: Flagellar motor switch protein FliN
D2: Flagellar motor switch protein FliM
D3: Flagellar motor switch protein FliG
D4: Chemotaxis protein CheY
D5: Flagellar motor switch protein FliN
D6: Flagellar motor switch protein FliN
D7: Flagellar motor switch protein FliN
D8: Flagellar motor switch protein FliM
D9: Flagellar motor switch protein FliG
D0: Chemotaxis protein CheY
EA: Flagellar motor switch protein FliN
EB: Flagellar motor switch protein FliN
B0: Flagellar M-ring protein
B1: Flagellar motor switch protein FliN
B2: Flagellar motor switch protein FliN
B3: Flagellar M-ring protein
B4: Flagellar motor switch protein FliM
B5: Flagellar motor switch protein FliG
B6: Chemotaxis protein CheY
B7: Flagellar motor switch protein FliN
B8: Flagellar motor switch protein FliN
B9: Flagellar motor switch protein FliN
EC: Flagellar motor switch protein FliG
ED: Chemotaxis protein CheY
EE: Flagellar motor switch protein FliN
EF: Flagellar motor switch protein FliN
EG: Flagellar motor switch protein FliN
EH: Flagellar M-ring protein
EI: Flagellar motor switch protein FliM
EJ: Flagellar motor switch protein FliG
EK: Chemotaxis protein CheY
EL: Flagellar motor switch protein FliN
EM: Flagellar motor switch protein FliN
EN: Flagellar motor switch protein FliN
EO: Flagellar M-ring protein
EP: Flagellar motor switch protein FliM
EQ: Flagellar motor switch protein FliG
ER: Chemotaxis protein CheY
ES: Flagellar motor switch protein FliN
ET: Flagellar motor switch protein FliN
EU: Flagellar motor switch protein FliN
EV: Flagellar M-ring protein
EW: Flagellar motor switch protein FliM
EX: Flagellar motor switch protein FliG
EY: Chemotaxis protein CheY
EZ: Flagellar motor switch protein FliN
BY: Flagellar motor switch protein FliN
BZ: Flagellar motor switch protein FliN
Ba: Flagellar M-ring protein
Bb: Flagellar motor switch protein FliM
Bc: Flagellar motor switch protein FliG
Bd: Chemotaxis protein CheY
Be: Flagellar motor switch protein FliN
Bf: Flagellar motor switch protein FliN
Bg: Flagellar motor switch protein FliN
Bh: Flagellar M-ring protein
Bi: Flagellar motor switch protein FliM
Bj: Flagellar motor switch protein FliG
Bk: Chemotaxis protein CheY
Bl: Flagellar motor switch protein FliN
Bm: Flagellar motor switch protein FliN
Bn: Flagellar motor switch protein FliN
Bo: Flagellar M-ring protein
Bp: Flagellar motor switch protein FliM
Bq: Flagellar motor switch protein FliG
Br: Chemotaxis protein CheY
Bs: Flagellar motor switch protein FliN
Bt: Flagellar motor switch protein FliN
Bu: Flagellar motor switch protein FliN
Bv: Flagellar M-ring protein
Bw: Flagellar motor switch protein FliM
Bx: Flagellar motor switch protein FliG
By: Chemotaxis protein CheY
Bz: Flagellar motor switch protein FliN
Ea: Flagellar M-ring protein
C1: Flagellar motor switch protein FliN
C2: Flagellar motor switch protein FliN
CA: Flagellar motor switch protein FliM
CB: Flagellar motor switch protein FliG
CC: Chemotaxis protein CheY
CD: Flagellar motor switch protein FliN
CE: Flagellar motor switch protein FliN
CF: Flagellar motor switch protein FliN
CG: Flagellar M-ring protein
CH: Flagellar motor switch protein FliM
CI: Flagellar motor switch protein FliG
CJ: Chemotaxis protein CheY
CK: Flagellar motor switch protein FliN
CL: Flagellar motor switch protein FliN
CM: Flagellar motor switch protein FliN
CN: Flagellar M-ring protein
CO: Flagellar motor switch protein FliM
CP: Flagellar motor switch protein FliG
CQ: Chemotaxis protein CheY
CR: Flagellar motor switch protein FliN
CS: Flagellar motor switch protein FliN
CT: Flagellar motor switch protein FliN
CU: Flagellar M-ring protein
CV: Flagellar motor switch protein FliM
CW: Flagellar motor switch protein FliG
CX: Chemotaxis protein CheY
CY: Flagellar motor switch protein FliN
CZ: Flagellar motor switch protein FliN
Ca: Flagellar motor switch protein FliN
Cb: Flagellar M-ring protein
Cc: Flagellar motor switch protein FliM
Cd: Flagellar motor switch protein FliG
Ce: Chemotaxis protein CheY
Cf: Flagellar motor switch protein FliN
Cg: Flagellar motor switch protein FliN
Ch: Flagellar motor switch protein FliN
Ci: Flagellar M-ring protein
Cj: Flagellar motor switch protein FliM
Ck: Flagellar motor switch protein FliG
Cl: Chemotaxis protein CheY
Cm: Flagellar motor switch protein FliN
Cn: Flagellar motor switch protein FliN
Co: Flagellar motor switch protein FliN
Cp: Flagellar M-ring protein
Cq: Flagellar motor switch protein FliM
Cr: Flagellar motor switch protein FliG
Cs: Chemotaxis protein CheY
Ct: Flagellar motor switch protein FliN
Cu: Flagellar motor switch protein FliN
Cv: Flagellar motor switch protein FliN
Cw: Flagellar M-ring protein
Cx: Flagellar motor switch protein FliM
Cy: Flagellar motor switch protein FliG
Cz: Chemotaxis protein CheY
Eb: Flagellar M-ring protein
Ec: Flagellar M-ring protein
Ed: Flagellar M-ring protein
Ee: Flagellar M-ring protein
Ef: Flagellar M-ring protein
Eg: Flagellar M-ring protein
Eh: Flagellar M-ring protein
Ei: Flagellar M-ring protein
Ej: Flagellar M-ring protein
Ek: Flagellar M-ring protein
El: Flagellar M-ring protein
Em: Flagellar M-ring protein
En: Flagellar M-ring protein
Eo: Flagellar M-ring protein
Ep: Flagellar M-ring protein
Eq: Flagellar motor switch protein FliM
Er: Flagellar motor switch protein FliM
Es: Flagellar motor switch protein FliM
Et: Flagellar motor switch protein FliM
Eu: Flagellar motor switch protein FliM
Ev: Flagellar motor switch protein FliM
Ew: Flagellar motor switch protein FliM
Ex: Flagellar motor switch protein FliG
Ey: Flagellar motor switch protein FliG
Ez: Flagellar motor switch protein FliG
E1: Flagellar motor switch protein FliG
E2: Flagellar motor switch protein FliG
E3: Flagellar motor switch protein FliG
E4: Flagellar motor switch protein FliG
E5: Flagellar motor switch protein FliM
E6: Chemotaxis protein CheY
E7: Chemotaxis protein CheY
E8: Chemotaxis protein CheY
E9: Chemotaxis protein CheY
E0: Chemotaxis protein CheY
FA: Chemotaxis protein CheY
FB: Chemotaxis protein CheY
FC: Flagellar motor switch protein FliN
FD: Flagellar motor switch protein FliN
FE: Flagellar motor switch protein FliN
FF: Flagellar motor switch protein FliN
FG: Flagellar motor switch protein FliN
FH: Flagellar motor switch protein FliN
FI: Flagellar motor switch protein FliN
FJ: Flagellar motor switch protein FliN
FK: Flagellar motor switch protein FliN
FL: Flagellar motor switch protein FliN
FM: Flagellar motor switch protein FliN
FN: Flagellar motor switch protein FliN


Theoretical massNumber of molelcules
Total (without water)15,362,990451
Polymers15,362,990451
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Flagellar basal-body rod protein ... , 3 types, 35 molecules 0123456789AFAGAHAIAJAKALAMANZAZBZCZDZEAAABACADAEBA...

#1: Protein ...
Flagellar basal-body rod protein FlgG / Distal rod protein


Mass: 27784.807 Da / Num. of mol.: 24 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P0A1J3
#5: Protein
Flagellar basal-body rod protein FlgF / Putative proximal rod protein


Mass: 26121.223 Da / Num. of mol.: 5 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P16323
#10: Protein
Flagellar basal-body rod protein FlgC / Putative proximal rod protein


Mass: 13991.889 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P0A1I7

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Protein , 7 types, 236 molecules ABCDEFGHIJKLMNOPQRSTUVWXYZA0A6A7A8...

#2: Protein ...
Flagellar L-ring protein / Basal body L-ring protein


Mass: 24726.666 Da / Num. of mol.: 26 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P0A1N8
#3: Protein
Flagellar basal body rod protein FlgB / Putative proximal rod protein


Mass: 15145.061 Da / Num. of mol.: 5 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P16437
#4: Protein
Flagellar hook-basal body complex protein FliE


Mass: 11087.662 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P26462
#6: Protein ...
Flagellar M-ring protein


Mass: 61295.645 Da / Num. of mol.: 110 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P15928
#11: Protein ...
Flagellar hook protein FlgE


Mass: 42233.152 Da / Num. of mol.: 29 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P0A1J1
#12: Protein ...
Flagellar P-ring protein / Basal body P-ring protein


Mass: 38194.176 Da / Num. of mol.: 26 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P15930
#15: Protein ...
Chemotaxis protein CheY


Mass: 14177.512 Da / Num. of mol.: 34 / Mutation: D13K, Y106W
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Gene: cheY, STM1916 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A2D5

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Flagellar biosynthetic protein ... , 3 types, 10 molecules AbAqArAsAtAuAvAwAxAy

#7: Protein
Flagellar biosynthetic protein FliQ


Mass: 9606.758 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P0A1L5
#8: Protein Flagellar biosynthetic protein FliR


Mass: 28938.865 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P54702
#9: Protein
Flagellar biosynthetic protein FliP


Mass: 26801.086 Da / Num. of mol.: 5 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P54700

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Flagellar motor switch protein ... , 3 types, 170 molecules C3C4C5C8C9DDDIDJDKDMDNDODPDQDRDSDTDUDVDWDaDbDcDgDhDiDmDnDoDs...

#13: Protein ...
Flagellar motor switch protein FliN


Mass: 14801.823 Da / Num. of mol.: 102 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P26419
#14: Protein ...
Flagellar motor switch protein FliG


Mass: 36890.957 Da / Num. of mol.: 34 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P0A1J9
#16: Protein ...
Flagellar motor switch protein FliM


Mass: 37901.066 Da / Num. of mol.: 34 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P26418

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: C ring-containing flagellar motor-hook complex in the CW state
Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Molecular weightExperimental value: NO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Source (recombinant)Organism: Escherichia coli BL21(DE3) (bacteria)
Buffer solutionpH: 8
Buffer component
IDConc.NameFormulaBuffer-ID
111.7 mMtris(hydroxymethyl)aminomethane hydrochlorideTris-HCl1
24.17 mMethylenediaminetetraacetic acidEDTA1
30.083 % v/voctylphenol ethoxylateTX-1001
425 mMsodium chlorideNaCl1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: This sample was prepared by incubating the C ring-containing flagellar motor-hook complex with the constitutively active mutant of CheY (CheY**)
Specimen supportGrid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R0.6/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K
Details: Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm / Cs: 2.7 mm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)
EM imaging opticsEnergyfilter name: TFS Selectris / Energyfilter slit width: 10 eV

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.1.1particle selection
2EPUimage acquisition
4cryoSPARC4.1.1CTF correction
7UCSF Chimera1.17model fitting
8UCSF ChimeraX1.5model fitting
10cryoSPARC4.1.1initial Euler assignment
11cryoSPARC4.1.1final Euler assignment
13cryoSPARC4.1.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 46058 / Details: Particles were manually picked using cryoSPARC
SymmetryPoint symmetry: C34 (34 fold cyclic)
3D reconstructionResolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 26921 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT
Atomic model building
ID 3D fitting-IDDetailsSource nameTypeAccession codeInitial refinement model-ID
11Model-AngeloOtherin silico model
21AlphaFoldin silico model
31PDBexperimental model7CBL3
41PDBexperimental model7CGO

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