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- PDB-6j5k: Cryo-EM structure of the mammalian ATP synthase tetramer bound wi... -

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Entry
Database: PDB / ID: 6j5k
TitleCryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1
Components
  • (ATP synthase ...) x 15
  • ATP synthase-coupling factor 6, mitochondrial
  • ATPase inhibitor, mitochondrial
  • Mitochondrial H+ transporting ATP synthase subunit c isoform 1
  • subunit k analog
KeywordsMEMBRANE PROTEIN
Function / homology
Function and homology information


Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex binding / regulation of ATP metabolic process / regulation of protein targeting to mitochondrion / positive regulation of proteolysis involved in protein catabolic process / positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization / Mitochondrial protein import / angiostatin binding / ATPase inhibitor activity ...Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex binding / regulation of ATP metabolic process / regulation of protein targeting to mitochondrion / positive regulation of proteolysis involved in protein catabolic process / positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization / Mitochondrial protein import / angiostatin binding / ATPase inhibitor activity / mitochondrial depolarization / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / negative regulation of hydrolase activity / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / heme biosynthetic process / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / negative regulation of endothelial cell proliferation / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / reactive oxygen species metabolic process / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / erythrocyte differentiation / ADP binding / mitochondrial membrane / ATPase binding / calmodulin binding / lipid binding / cell surface / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / identical protein binding / plasma membrane
Similarity search - Function
ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase protein 8, metazoa / Mitochondrial F1-F0 ATP synthase subunit F, predicted / ATP synthase protein 8, mammals / ATP synthase protein 8 / Mitochondrial F1F0-ATP synthase, subunit f / Mitochondrial ATPase inhibitor / Mitochondrial ATPase inhibitor, IATP / ATP synthase-coupling factor 6, mitochondrial ...ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase protein 8, metazoa / Mitochondrial F1-F0 ATP synthase subunit F, predicted / ATP synthase protein 8, mammals / ATP synthase protein 8 / Mitochondrial F1F0-ATP synthase, subunit f / Mitochondrial ATPase inhibitor / Mitochondrial ATPase inhibitor, IATP / ATP synthase-coupling factor 6, mitochondrial / ATP synthase-coupling factor 6 superfamily, mitochondrial / Mitochondrial ATP synthase coupling factor 6 / : / Metazoan delta subunit of F1F0-ATP synthase, C-terminal domain / ATP synthase delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F0 complex, subunit B/MI25 / ATP synthase, F0 complex, subunit B / Mitochondrial ATP synthase B chain precursor (ATP-synt_B) / ATP synthase, F0 complex, subunit D, mitochondrial / ATP synthase D chain, mitochondrial (ATP5H) / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / ATP synthase, F0 complex, subunit A, bacterial/mitochondria / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATPase, OSCP/delta subunit, conserved site / ATP synthase delta (OSCP) subunit signature. / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily / ATP synthase A chain / ATP synthase a subunit signature. / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / ATP synthase F1 subunit delta / ATP synthase subunit b / ATP synthase subunit gamma / ATP synthase subunit d, mitochondrial / ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit / ATP synthase membrane subunit K, mitochondrial / ATP synthase subunit beta / ATP synthase-coupling factor 6, mitochondrial ...ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / ATP synthase F1 subunit delta / ATP synthase subunit b / ATP synthase subunit gamma / ATP synthase subunit d, mitochondrial / ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit / ATP synthase membrane subunit K, mitochondrial / ATP synthase subunit beta / ATP synthase-coupling factor 6, mitochondrial / ATP synthase subunit alpha, mitochondrial / ATPase inhibitor, mitochondrial / ATP synthase subunit O, mitochondrial / ATP synthase protein 8 / ATP synthase subunit a / ATP synthase lipid-binding protein / ATP synthase subunit f, mitochondrial
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.2 Å
AuthorsGu, J. / Zhang, L. / Yi, J. / Yang, M.
Funding support China, 3items
OrganizationGrant numberCountry
Ministry of Science and Technology (China)2017YFA0504600 and 2016YFA0501100 China
National Natural Science Foundation of China31625008 China
National Natural Science Foundation of China21532004, 31570733 and 31800620 China
CitationJournal: Science / Year: 2019
Title: Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.
Authors: Jinke Gu / Laixing Zhang / Shuai Zong / Runyu Guo / Tianya Liu / Jingbo Yi / Peiyi Wang / Wei Zhuo / Maojun Yang /
Abstract: The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom ...The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-Å resolution.
History
DepositionJan 11, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 26, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 6, 2019Group: Data collection / Other / Category: cell / Item: _cell.Z_PDB
Revision 1.2Mar 27, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id

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Assembly

Deposited unit
A: ATP synthase F1 subunit alpha
B: ATP synthase F1 subunit alpha
C: ATP synthase F1 subunit alpha
D: ATP synthase subunit beta
E: ATP synthase subunit beta
F: ATP synthase subunit beta
J: ATPase inhibitor, mitochondrial
G: ATP synthase subunit gamma
H: ATP synthase subunit delta, mitochondrial
I: ATP synthase F1 subunit epsilon
S: ATP synthase subunit O, mitochondrial
b: ATP synthase peripheral stalk-membrane subunit b
c: ATP synthase-coupling factor 6, mitochondrial
d: ATP synthase subunit d, mitochondrial
e: ATP synthase subunit e
f: ATP synthase subunit f, mitochondrial
g: ATP synthase subunit g
i: ATP synthase membrane subunit DAPIT
k: subunit k analog
8: ATP synthase protein 8
a: ATP synthase subunit a
K: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
L: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
M: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
N: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
O: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
P: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
Q: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
R: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
u: ATP synthase membrane subunit 6.8PL
AA: ATP synthase F1 subunit alpha
AB: ATP synthase F1 subunit alpha
AC: ATP synthase F1 subunit alpha
AD: ATP synthase subunit beta
AE: ATP synthase subunit beta
AF: ATP synthase subunit beta
AJ: ATPase inhibitor, mitochondrial
AG: ATP synthase subunit gamma
AH: ATP synthase subunit delta, mitochondrial
AI: ATP synthase F1 subunit epsilon
AS: ATP synthase subunit O, mitochondrial
Ab: ATP synthase peripheral stalk-membrane subunit b
Ac: ATP synthase-coupling factor 6, mitochondrial
Ad: ATP synthase subunit d, mitochondrial
Ae: ATP synthase subunit e
Af: ATP synthase subunit f, mitochondrial
Ag: ATP synthase subunit g
Ai: ATP synthase membrane subunit DAPIT
Ak: subunit k analog
A8: ATP synthase protein 8
Aa: ATP synthase subunit a
AK: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AL: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AM: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AN: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AO: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AP: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AQ: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
AR: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
Au: ATP synthase membrane subunit 6.8PL
BA: ATP synthase F1 subunit alpha
BB: ATP synthase F1 subunit alpha
BC: ATP synthase F1 subunit alpha
BD: ATP synthase subunit beta
BE: ATP synthase subunit beta
BF: ATP synthase subunit beta
BJ: ATPase inhibitor, mitochondrial
BG: ATP synthase subunit gamma
BH: ATP synthase subunit delta, mitochondrial
BI: ATP synthase F1 subunit epsilon
BS: ATP synthase subunit O, mitochondrial
Bb: ATP synthase peripheral stalk-membrane subunit b
Bc: ATP synthase-coupling factor 6, mitochondrial
Bd: ATP synthase subunit d, mitochondrial
Be: ATP synthase subunit e
Bf: ATP synthase subunit f, mitochondrial
Bg: ATP synthase subunit g
Bi: ATP synthase membrane subunit DAPIT
Bk: subunit k analog
B8: ATP synthase protein 8
Ba: ATP synthase subunit a
BK: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BL: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BM: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BN: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BO: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BP: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BQ: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
BR: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
Bu: ATP synthase membrane subunit 6.8PL
CA: ATP synthase F1 subunit alpha
CB: ATP synthase F1 subunit alpha
CC: ATP synthase F1 subunit alpha
CD: ATP synthase subunit beta
CE: ATP synthase subunit beta
CF: ATP synthase subunit beta
CJ: ATPase inhibitor, mitochondrial
CG: ATP synthase subunit gamma
CH: ATP synthase subunit delta, mitochondrial
CI: ATP synthase F1 subunit epsilon
CS: ATP synthase subunit O, mitochondrial
Cb: ATP synthase peripheral stalk-membrane subunit b
Cc: ATP synthase-coupling factor 6, mitochondrial
Cd: ATP synthase subunit d, mitochondrial
Ce: ATP synthase subunit e
Cf: ATP synthase subunit f, mitochondrial
Cg: ATP synthase subunit g
Ci: ATP synthase membrane subunit DAPIT
Ck: subunit k analog
C8: ATP synthase protein 8
Ca: ATP synthase subunit a
CK: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CL: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CM: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CN: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CO: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CP: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CQ: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
CR: Mitochondrial H+ transporting ATP synthase subunit c isoform 1
Cu: ATP synthase membrane subunit 6.8PL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)2,294,307160
Polymers2,284,317120
Non-polymers9,99040
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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ATP synthase ... , 15 types, 76 molecules ABCAAABACBABBBCCACBCCDEFADAEAFBDBEBFCDCECFGAGBGCGHAH...

#1: Protein
ATP synthase F1 subunit alpha / ATP synthase subunit alpha / mitochondrial


Mass: 55171.105 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P80021
#2: Protein
ATP synthase subunit beta /


Mass: 50606.652 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig)
References: UniProt: K7GLT8, H+-transporting two-sector ATPase
#4: Protein
ATP synthase subunit gamma /


Mass: 30121.650 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A0A287A9I8
#5: Protein
ATP synthase subunit delta, mitochondrial /


Mass: 13852.506 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A0A286ZYL7
#6: Protein/peptide
ATP synthase F1 subunit epsilon / ATP synthase / H+ transporting / mitochondrial F1 complex / epsilon subunit


Mass: 5371.264 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A5GFX4
#7: Protein
ATP synthase subunit O, mitochondrial / / ATP synthase peripheral stalk subunit OSCP


Mass: 20561.279 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q2EN81
#8: Protein
ATP synthase peripheral stalk-membrane subunit b


Mass: 24002.934 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A0A286ZYM6
#10: Protein
ATP synthase subunit d, mitochondrial /


Mass: 16904.473 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A0A287B4I0
#11: Protein
ATP synthase subunit e /


Mass: 5379.623 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig)
#12: Protein
ATP synthase subunit f, mitochondrial / / ATP synthase membrane subunit f


Mass: 10197.959 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q95339
#13: Protein
ATP synthase subunit g /


Mass: 7166.825 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig)
#14: Protein/peptide
ATP synthase membrane subunit DAPIT


Mass: 4861.770 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: F1RFD4
#16: Protein
ATP synthase protein 8 / / A6L / F-ATPase subunit 8


Mass: 7954.407 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q35914
#17: Protein
ATP synthase subunit a / / F-ATPase protein 6


Mass: 25054.143 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q35915
#19: Protein/peptide
ATP synthase membrane subunit 6.8PL


Mass: 3592.419 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig)

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Protein , 3 types, 40 molecules JAJBJCJcAcBcCcKLMNOPQRAKALAMANAOAPAQARBKBLBMBNBOBP...

#3: Protein
ATPase inhibitor, mitochondrial / ATP synthase F1 subunit epsilon / Inhibitor of F(1)F(o)-ATPase / IF1


Mass: 9500.476 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q29307
#9: Protein
ATP synthase-coupling factor 6, mitochondrial / ATPase subunit F6 / ATP synthase peripheral stalk subunit F6


Mass: 8245.269 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P13618
#18: Protein ...
Mitochondrial H+ transporting ATP synthase subunit c isoform 1


Mass: 7311.631 Da / Num. of mol.: 32 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q4VT52

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Protein/peptide , 1 types, 4 molecules kAkBkCk

#15: Protein/peptide
subunit k analog


Mass: 2486.056 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig)

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Non-polymers , 3 types, 40 molecules

#20: Chemical
ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP, energy-carrying molecule*YM
#21: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#22: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM

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Details

Has ligand of interestY
Sequence detailsThe sequence of the chain e corresponds to Q03654 in the UniProt database. The sequence of the ...The sequence of the chain e corresponds to Q03654 in the UniProt database. The sequence of the chain g corresponds to A0A480XS10 in the UniProt database. The sequence of the chain u corresponds to F1S9V7 in the UniProt database. However, there are UNK (unknown residues) in these chains, as the authors do not know how the coordinates align with the sequences. Therefore the residues numbers are meaningless. As for k chain, the authors don't know the reference sequence in the UniProt database.

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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: Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1
Type: COMPLEX / Entity ID: #1-#19 / Source: NATURAL
Source (natural)Organism: Sus scrofa (pig)
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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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: OTHER
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 1.56 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 170000 / Symmetry type: POINT

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