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- PDB-8wln: Cryo-EM structure of the MS ring with export apparatus and proxim... -

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Basic information

Entry
Database: PDB / ID: 8wln
TitleCryo-EM structure of the MS ring with export apparatus and proximal rod within the motor-hook complex in the CCW state
Components
  • (Flagellar biosynthetic protein ...) x 3
  • Flagellar M-ring protein
  • Flagellar basal body rod protein FlgB
  • Flagellar basal-body rod protein FlgC
  • Flagellar hook-basal body complex protein FliE
KeywordsMOTOR PROTEIN / Flagellum / Flagellar motor
Function / homology
Function and homology information


bacterial-type flagellum basal body, rod / bacterial-type flagellum organization / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / bacterial-type flagellum assembly / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / protein secretion / protein targeting ...bacterial-type flagellum basal body, rod / bacterial-type flagellum organization / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / bacterial-type flagellum assembly / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / protein secretion / protein targeting / structural molecule activity / plasma membrane
Similarity search - Function
Flagellar basal-body rod protein FlgC / Flagellar hook-basal body complex protein FliE / Flagellar basal-body rod protein FlgB / Flagellar hook-basal body complex protein FliE / Flagellar biosynthesis protein FliQ / Flagellar biosynthesis protein FliR / Flagellar transport protein FliP / Type III secretion system inner membrane R protein / Bacterial export protein family 3 / Bacterial export proteins, family 1 ...Flagellar basal-body rod protein FlgC / Flagellar hook-basal body complex protein FliE / Flagellar basal-body rod protein FlgB / Flagellar hook-basal body complex protein FliE / Flagellar biosynthesis protein FliQ / Flagellar biosynthesis protein FliR / Flagellar transport protein FliP / Type III secretion system inner membrane R protein / Bacterial export protein family 3 / Bacterial export proteins, family 1 / Bacterial export proteins, family 3 / Flagella transport protein fliP family signature 1. / Type III secretion system inner membrane P protein / FliP family / 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
Similarity search - Domain/homology
Flagellar basal-body rod protein FlgC / Flagellar biosynthetic protein FliQ / Flagellar M-ring protein / Flagellar basal body rod protein FlgB / 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: To Be Published
Title: Cryo-EM structure of the MS ring with export apparatus and proximal rod within the motor-hook complex in the CCW state
Authors: Tan, J.X. / Zhang, L. / Zhou, Y. / Zhu, Y.Q.
History
DepositionSep 30, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 4, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: Flagellar M-ring protein
1: Flagellar M-ring protein
2: Flagellar M-ring protein
3: Flagellar M-ring protein
4: Flagellar M-ring protein
5: Flagellar M-ring protein
6: Flagellar M-ring protein
7: Flagellar M-ring protein
8: Flagellar M-ring protein
9: Flagellar M-ring protein
AA: Flagellar M-ring protein
AB: Flagellar M-ring protein
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 M-ring protein
K: Flagellar hook-basal body complex protein FliE
L: Flagellar hook-basal body complex protein FliE
M: Flagellar hook-basal body complex protein FliE
N: Flagellar hook-basal body complex protein FliE
O: Flagellar hook-basal body complex protein FliE
P: Flagellar hook-basal body complex protein FliE
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
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
t: Flagellar M-ring protein
u: Flagellar M-ring protein
v: Flagellar M-ring protein
w: Flagellar M-ring protein
x: Flagellar M-ring protein
y: Flagellar M-ring protein
z: Flagellar M-ring protein
A: Flagellar biosynthetic protein FliQ
B: Flagellar biosynthetic protein FliQ
C: Flagellar biosynthetic protein FliQ
D: Flagellar biosynthetic protein FliQ
E: Flagellar biosynthetic protein FliR
F: Flagellar biosynthetic protein FliP
G: Flagellar biosynthetic protein FliP
H: Flagellar biosynthetic protein FliP
I: Flagellar biosynthetic protein FliP
J: Flagellar biosynthetic protein FliP
Q: Flagellar basal body rod protein FlgB
R: Flagellar basal body rod protein FlgB
S: Flagellar basal body rod protein FlgB
T: Flagellar basal body rod protein FlgB
U: Flagellar basal body rod protein FlgB
V: Flagellar basal-body rod protein FlgC
W: Flagellar basal-body rod protein FlgC
X: Flagellar basal-body rod protein FlgC
Y: Flagellar basal-body rod protein FlgC
Z: Flagellar basal-body rod protein FlgC
a: Flagellar basal-body rod protein FlgC
b: Flagellar M-ring protein
c: Flagellar M-ring protein
d: Flagellar M-ring protein
e: Flagellar M-ring protein
f: Flagellar M-ring protein
g: Flagellar M-ring protein
h: Flagellar M-ring protein
i: Flagellar M-ring protein
j: Flagellar M-ring protein
k: Flagellar M-ring protein
l: Flagellar M-ring protein


Theoretical massNumber of molelcules
Total (without water)5,086,043103
Polymers5,086,043103
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 4 types, 93 molecules 0123456789AAABACADAEAFAGAHAIAJAKALAMANAOAPAQUIUJUK...

#1: Protein ...
Flagellar M-ring protein


Mass: 61295.645 Da / Num. of mol.: 76 / Source method: isolated from a natural source
Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
References: UniProt: P15928
#2: 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 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
#7: 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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Flagellar biosynthetic protein ... , 3 types, 10 molecules ABCDEFGHIJ

#3: 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
#4: 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
#5: 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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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 CCW state
Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Buffer solutionpH: 8
Buffer component
IDConc.NameFormulaBuffer-ID
110 mMtris(hydroxymethyl)aminomethane hydrochlorideTris-HCl1
25 mMethylenediaminetetraacetic acidEDTA1
30.1 % v/voctylphenol ethoxylateTX-1001
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K
Details: Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1

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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: 2500 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm
Image recordingElectron dose: 45 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.1.1particle selection
2SerialEMimage acquisition
4cryoSPARC4.1.1CTF correction
7UCSF Chimera1.17model fitting
8UCSF ChimeraX1.5model fitting
9Coot0.9.8.7model fitting
11cryoSPARC4.1.1initial Euler assignment
12cryoSPARC4.1.1final Euler assignment
14cryoSPARC4.1.13D reconstruction
15PHENIX1.20.1_4487:model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 22192 / Details: Particles were manually picked using cryoSPARC
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 11858 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
Atomic model building
ID 3D fitting-IDSource nameTypeDetailsAccession code
11AlphaFoldin silico model
21Otherin silico modelModel-Angelo
31PDBexperimental model7CGO

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