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- PDB-6oqs: E. coli ATP synthase State 1b -

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Basic information

Entry
Database: PDB / ID: 6oqs
TitleE. coli ATP synthase State 1b
Components(ATP synthase ...) x 8
KeywordsMEMBRANE PROTEIN / F1Fo ATP synthase
Function / homology
Function and homology information


proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / hydrolase activity ...proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / hydrolase activity / lipid binding / ATP hydrolysis activity / ATP binding / membrane / plasma membrane
Similarity search - Function
ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / ATP synthase alpha/beta chain, C-terminal domain / F1F0 ATP synthase subunit C / F1FO ATP Synthase / Lysin / Thrombin, subunit H - #170 ...ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / ATP synthase alpha/beta chain, C-terminal domain / F1F0 ATP synthase subunit C / F1FO ATP Synthase / Lysin / Thrombin, subunit H - #170 / Elongation Factor Tu (Ef-tu); domain 3 - #20 / Pyruvate Kinase; Chain: A, domain 1 / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / ATP synthase, gamma subunit, helix hairpin domain / ATP synthase, F0 complex, subunit b, bacterial / F-type ATP synthase subunit B-like, membrane domain superfamily / : / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0) / ATP synthase delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / 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 / C-terminal domain of V and A type ATP synthase / 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. / Elongation Factor Tu (Ef-tu); domain 3 / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Helix Hairpins / Thrombin, subunit H / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Up-down Bundle / Beta Barrel / Sandwich / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / PHOSPHATE ION / ATP synthase subunit alpha / : / ATP synthase epsilon chain / ATP synthase subunit a / ATP synthase subunit b / ATP synthase subunit c / ATP synthase gamma chain ...ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / PHOSPHATE ION / ATP synthase subunit alpha / : / ATP synthase epsilon chain / ATP synthase subunit a / ATP synthase subunit b / ATP synthase subunit c / ATP synthase gamma chain / ATP synthase epsilon chain / ATP synthase subunit a / ATP synthase subunit b / ATP synthase subunit delta / ATP synthase gamma chain / ATP synthase subunit alpha / ATP synthase subunit beta / ATP synthase subunit c / ATP synthase subunit delta
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsStewart, A.G. / Sobti, M. / Walshe, J.L.
Funding support Australia, 1items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia) Australia
CitationJournal: Nat Commun / Year: 2020
Title: Cryo-EM structures provide insight into how E. coli FF ATP synthase accommodates symmetry mismatch.
Authors: Meghna Sobti / James L Walshe / Di Wu / Robert Ishmukhametov / Yi C Zeng / Carol V Robinson / Richard M Berry / Alastair G Stewart /
Abstract: FF ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a ...FF ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a peripheral stalk. Proton flow through the F motor generates rotation of the central stalk, inducing conformational changes in the F motor that catalyzes ATP production. Here we present nine cryo-EM structures of E. coli ATP synthase to 3.1-3.4 Å resolution, in four discrete rotational sub-states, which provide a comprehensive structural model for this widely studied bacterial molecular machine. We observe torsional flexing of the entire complex and a rotational sub-step of F associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F and F motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the F motor.
History
DepositionApr 29, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 3, 2020Provider: repository / Type: Initial release
Revision 1.1Jun 10, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jun 24, 2020Group: Data processing / Structure summary / Category: audit_author / em_3d_reconstruction
Item: _audit_author.name / _em_3d_reconstruction.num_particles / _em_3d_reconstruction.resolution
Revision 1.3Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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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Structure visualization

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Assembly

Deposited unit
W: ATP synthase subunit delta
C: ATP synthase subunit alpha
B: ATP synthase subunit alpha
A: ATP synthase subunit alpha
X: ATP synthase subunit b
H: ATP synthase epsilon chain
G: ATP synthase gamma chain
F: ATP synthase subunit beta
E: ATP synthase subunit beta
D: ATP synthase subunit beta
I: ATP synthase subunit c
J: ATP synthase subunit c
L: ATP synthase subunit c
M: ATP synthase subunit c
N: ATP synthase subunit c
O: ATP synthase subunit c
P: ATP synthase subunit c
Q: ATP synthase subunit c
R: ATP synthase subunit c
S: ATP synthase subunit c
Y: ATP synthase subunit b
a: ATP synthase subunit a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)537,26934
Polymers534,25022
Non-polymers3,02012
Water00
1


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

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Components

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ATP synthase ... , 8 types, 22 molecules WCBAXYHGFEDIJLMNOPQRSa

#1: Protein ATP synthase subunit delta / ATP synthase F(1) sector subunit delta / F-type ATPase subunit delta / F-ATPase subunit delta


Mass: 19289.061 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: atpH, HMPREF1611_00658 / Production host: Escherichia coli (E. coli) / References: UniProt: V0ZA15, UniProt: P0ABA4*PLUS
#2: Protein ATP synthase subunit alpha / ATP synthase F1 sector subunit alpha / F-ATPase subunit alpha


Mass: 55281.871 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli / Gene: atpA, AD31_4476 / Production host: Escherichia coli (E. coli)
References: UniProt: A0A073FQ32, UniProt: P0ABB0*PLUS, H+-transporting two-sector ATPase
#3: Protein ATP synthase subunit b / ATP synthase F(0) sector subunit b / ATPase subunit I / F-type ATPase subunit b / F-ATPase subunit b


Mass: 17289.953 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: atpf / Production host: Escherichia coli (E. coli) / References: UniProt: D6IFY0, UniProt: P0ABA0*PLUS
#4: Protein ATP synthase epsilon chain / ATP synthase F1 sector epsilon subunit / F-ATPase epsilon subunit


Mass: 15087.244 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli / Gene: atpC, CCU01_030215 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A4V1DSB5, UniProt: P0A6E6*PLUS
#5: Protein ATP synthase gamma chain / ATP synthase F1 sector gamma subunit / F-ATPase gamma subunit


Mass: 31539.285 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli / Gene: atpG, BN16_43751 / Production host: Escherichia coli (E. coli) / References: UniProt: J7RYJ3, UniProt: P0ABA6*PLUS
#6: Protein ATP synthase subunit beta / ATP synthase F1 sector subunit beta / F-ATPase subunit beta


Mass: 51664.574 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli / Gene: atpD, CDCO157_4410 / Production host: Escherichia coli (E. coli)
References: UniProt: A0A0F6CB56, UniProt: P0ABB4*PLUS, H+-transporting two-sector ATPase
#7: Protein
ATP synthase subunit c / ATP synthase F(0) sector subunit c / F-type ATPase subunit c / F-ATPase subunit c / Lipid-binding protein


Mass: 8259.064 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: atpE, ECJG_03465 / Production host: Escherichia coli (E. coli) / References: UniProt: F4TL55, UniProt: P68699*PLUS
#8: Protein ATP synthase subunit a / ATP synthase F0 sector subunit a / F-ATPase subunit 6


Mass: 30324.096 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: atpB, A6581_09625, A8C65_04635, A8G17_13205, A9819_21465, AC789_1c41260, ACN002_3840, ACN77_20010, ACN81_06510, ACU57_03300, ACU90_00315, AKG99_01200, AM464_11965, AMK83_17435, AML07_02005, ...Gene: atpB, A6581_09625, A8C65_04635, A8G17_13205, A9819_21465, AC789_1c41260, ACN002_3840, ACN77_20010, ACN81_06510, ACU57_03300, ACU90_00315, AKG99_01200, AM464_11965, AMK83_17435, AML07_02005, AML35_23925, APZ14_19970, AU473_02230, AUQ13_19445, AUS26_01135, AW059_18665, AW106_23235, B1K96_28785, B7C53_19560, BANRA_02401, BANRA_03128, BANRA_03214, BANRA_04536, BANRA_04611, BB545_21600, BHF46_03220, BHS81_22305, BIZ41_19310, BK292_20055, BK400_00980, BMT53_14990, BMT91_10650, BN17_36921, BTQ04_25560, BTQ06_19305, BUE81_18230, BVL39_06790, BW690_12705, BWP17_17405, BZL31_21415, C2U48_14255, C4J69_12205, C5N07_23075, C5P01_14375, C5P43_18495, C5P44_14015, C6669_08960, C7235_25075, C7B02_15545, C7B06_18115, C7B07_18555, CA593_07300, CG691_14695, CG692_21460, CG705_13230, CG706_05505, COD30_14545, COD46_05110, CR538_25535, CR539_00375, CRD98_06365, CRE06_22220, CRM83_19985, CV83915_02325, CVH05_22810, CWS33_22485, D0X26_21590, D2F89_18645, D3821_26125, D3I61_22220, D6Z21_17295, D7K63_14130, D8K42_12760, D9D20_15080, D9D23_18435, D9D65_17115, D9D69_04800, D9D77_23770, D9E35_19420, D9F57_04785, D9G42_23250, D9H12_19550, D9H53_20710, D9H66_14770, D9H68_12120, D9H70_07975, D9H84_13135, D9I18_08055, D9I52_22315, D9I93_11990, D9J11_15870, D9J44_15620, D9J48_14640, D9K10_12565, DIV22_14605, DL800_26315, DL925_10465, DLU27_05670, DM262_10125, DMI41_02740, DNQ45_04220, DOT75_06920, DP258_23940, DP277_10610, DQF57_16240, DS732_00235, DTL43_15450, DTL90_16085, DV750_19840, E2855_04743, EAI42_11905, EAI44_10320, EAI52_06435, EB510_22250, EB553_22600, EB569_11805, EB595_21530, EC1094V2_4559, EC3234A_68c00800, EC95NR1_03180, ECs4680, ED060_20795, ED098_20360, ED124_20405, ED133_14365, ED287_08070, ED600_20035, ED648_17305, ED653_18700, ED658_09750, ED944_14625, EEP03_14120, EEP23_14845, EF364_23525, EFV06_19295, EIA21_14165, EL75_4432, EL79_4683, EL80_4591, ERS085374_04660, ERS085379_02386, ERS085383_02615, ERS085386_04244, ERS085404_04407, ERS150876_04315, FORC28_6046, GJ11_23870, HW43_00205, JD73_04915, NCTC10090_03054, NCTC10418_07533, NCTC10429_00459, NCTC10444_05020, NCTC11022_03985, NCTC11126_01888, NCTC11181_02279, NCTC13125_03147, NCTC13127_06463, NCTC13462_03577, NCTC7152_05030, NCTC8179_05398, NCTC8622_01220, NCTC8960_02611, NCTC9036_04909, NCTC9037_05079, NCTC9045_05855, NCTC9054_05546, NCTC9055_01929, NCTC9058_01885, NCTC9062_03146, NCTC9073_06659, NCTC9111_05225, NCTC9117_06282, NCTC9119_05322, NCTC9701_05266, NCTC9703_04488, NCTC9706_02267, NCTC9969_05235, PU06_21025, RG28_23995, RK56_018685, RX35_03591, SAMEA3472044_00548, SAMEA3472047_02992, SAMEA3472055_04839, SAMEA3472056_03685, SAMEA3472067_04030, SAMEA3472070_05212, SAMEA3472080_03392, SAMEA3472108_02423, SAMEA3472114_05011, SAMEA3472147_03706, SAMEA3484427_03569, SAMEA3484429_03570, SAMEA3484433_04143, SAMEA3485101_04107, SAMEA3752557_01245, SAMEA3752559_04742, SAMEA3753064_05400, SAMEA3753097_00985, SAMEA3753290_05396, SAMEA3753300_04372, SAMEA3753397_02464, SK85_04068, UN86_05680, UN91_09915, WQ89_11300, WR15_16550
Production host: Escherichia coli (E. coli) / References: UniProt: C3SL77, UniProt: P0AB98*PLUS

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Non-polymers , 4 types, 12 molecules

#9: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#10: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#11: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#12: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4

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Details

Has ligand of interestN

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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: E. coli ATP synthase / Type: COMPLEX / Entity ID: #1-#8 / Source: RECOMBINANT
Molecular weightValue: 0.558 MDa / Experimental value: YES
Source (natural)Organism: Escherichia coli (E. coli)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: unspecified
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: FLOOD BEAM
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 48 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: dev_3758: / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35243 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00737527
ELECTRON MICROSCOPYf_angle_d0.70550796
ELECTRON MICROSCOPYf_dihedral_angle_d17.6715279
ELECTRON MICROSCOPYf_chiral_restr0.0455919
ELECTRON MICROSCOPYf_plane_restr0.0046550

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