2XQS
 
 | | Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases | | Descriptor: | ATP SYNTHASE C CHAIN, CYMAL-4 | | Authors: | Pogoryelov, D, Krah, A, Langer, J, Yildiz, O, Faraldo-Gomez, J.D, Meier, T. | | Deposit date: | 2010-09-07 | | Release date: | 2010-10-27 | | Last modified: | 2024-11-06 | | Method: | X-RAY DIFFRACTION (3 Å) | | Cite: | Microscopic Rotary Mechanism of Ion Translocation in the Fo Complex of ATP Synthases
Nat.Chem.Biol., 6, 2010
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2XQT
 | | Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases | | Descriptor: | ATP SYNTHASE C CHAIN, CYMAL-4, DICYCLOHEXYLUREA | | Authors: | Pogoryelov, D, Krah, A, Langer, J, Yildiz, O, Faraldo-Gomez, J.D, Meier, T. | | Deposit date: | 2010-09-07 | | Release date: | 2010-10-27 | | Last modified: | 2024-10-09 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Microscopic Rotary Mechanism of Ion Translocation in the Fo Complex of ATP Synthases
Nat.Chem.Biol., 6, 2010
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7VIL
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7XKZ
 | | Solution structure of subunit epsilon of the Mycobacterium abscessus F-ATP synthase | | Descriptor: | ATP synthase epsilon chain | | Authors: | Shin, J, Grueber, G, Harikishore, A, Wong, C.F, Prya, R, Dick, T. | | Deposit date: | 2022-04-20 | | Release date: | 2023-03-08 | | Last modified: | 2024-05-15 | | Method: | SOLUTION NMR | | Cite: | Atomic solution structure of Mycobacterium abscessus F-ATP synthase subunit epsilon and identification of Ep1MabF1 as a targeted inhibitor.
Febs J., 289, 2022
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4V1F
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4V1G
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3ND9
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3ND8
 | | Structural characterization for the nucleotide binding ability of subunit A of the A1AO ATP synthase | | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, ACETIC ACID, ... | | Authors: | Kumar, A, Gruber, G. | | Deposit date: | 2010-06-07 | | Release date: | 2011-03-30 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
J.Mol.Biol., 408, 2011
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5BQ6
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5BQA
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5BPS
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6YNY
 | | Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo composite dimer model | | Descriptor: | 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE, 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine, ADENOSINE-5'-DIPHOSPHATE, ... | | Authors: | Kock Flygaard, R, Muhleip, A, Amunts, A. | | Deposit date: | 2020-04-14 | | Release date: | 2020-09-30 | | Last modified: | 2020-11-11 | | Method: | ELECTRON MICROSCOPY (2.7 Å) | | Cite: | Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
Nat Commun, 11, 2020
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8JR1
 | | Cryo-EM structure of Mycobacterium tuberculosis ATP synthase Fo in complex with TBAJ-587 | | Descriptor: | (1~{S},2~{S})-1-(6-bromanyl-2-methoxy-quinolin-3-yl)-2-(2,6-dimethoxypyridin-4-yl)-4-(dimethylamino)-1-(2-fluoranyl-3-methoxy-phenyl)butan-2-ol, ATP synthase subunit a, ATP synthase subunit c | | Authors: | Zhang, Y, Lai, Y, Liu, F, Rao, Z, Gong, H. | | Deposit date: | 2023-06-15 | | Release date: | 2024-05-01 | | Last modified: | 2024-08-21 | | Method: | ELECTRON MICROSCOPY (3.17 Å) | | Cite: | Inhibition of M. tuberculosis and human ATP synthase by BDQ and TBAJ-587.
Nature, 631, 2024
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6RDA
 | | CryoEM structure of Polytomella F-ATP synthase, Primary rotary state 1, monomer-masked refinement | | Descriptor: | ASA-10: Polytomella F-ATP synthase associated subunit 10, ASA-2: Polytomella F-ATP synthase associated subunit 2, ASA-9: Polytomella F-ATP synthase associated subunit 9, ... | | Authors: | Murphy, B.J, Klusch, N, Yildiz, O, Kuhlbrandt, W. | | Deposit date: | 2019-04-12 | | Release date: | 2019-07-03 | | Last modified: | 2024-05-22 | | Method: | ELECTRON MICROSCOPY (3.04 Å) | | Cite: | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364, 2019
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6RDF
 | | CryoEM structure of Polytomella F-ATP synthase, Primary rotary state 3, monomer-masked refinement | | Descriptor: | ASA-10: Polytomella F-ATP synthase associated subunit 10, ASA-2: Polytomella F-ATP synthase associated subunit 2, ASA-9: Polytomella F-ATP synthase associated subunit 9, ... | | Authors: | Murphy, B.J, Klusch, N, Yildiz, O, Kuhlbrandt, W. | | Deposit date: | 2019-04-12 | | Release date: | 2019-07-03 | | Last modified: | 2024-05-22 | | Method: | ELECTRON MICROSCOPY (3.2 Å) | | Cite: | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364, 2019
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6RD7
 | | CryoEM structure of Polytomella F-ATP synthase, c-ring position 1, focussed refinement of Fo and peripheral stalk | | Descriptor: | ASA-10: Polytomella F-ATP synthase associated subunit 10, ASA-9: Polytomella F-ATP synthase associated subunit 9, ATP synthase associated protein ASA1, ... | | Authors: | Murphy, B.J, Klusch, N, Yildiz, O, Kuhlbrandt, W. | | Deposit date: | 2019-04-12 | | Release date: | 2019-07-03 | | Last modified: | 2020-09-30 | | Method: | ELECTRON MICROSCOPY (2.73 Å) | | Cite: | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364, 2019
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6RDD
 | | Cryo-EM structure of Polytomella F-ATP synthase, Primary rotary state 2, monomer-masked refinement | | Descriptor: | ASA-10: Polytomella F-ATP synthase associated subunit 10, ATP synthase associated protein ASA1, ATP synthase subunit alpha, ... | | Authors: | Murphy, B.J, Klusch, N, Yildiz, O, Kuhlbrandt, W. | | Deposit date: | 2019-04-12 | | Release date: | 2019-07-03 | | Last modified: | 2024-05-22 | | Method: | ELECTRON MICROSCOPY (3.2 Å) | | Cite: | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364, 2019
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6RD8
 | | CryoEM structure of Polytomella F-ATP synthase, c-ring position 2, focussed refinement of Fo and peripheral stalk | | Descriptor: | ASA-10: Polytomella F-ATP synthase associated subunit 10, ASA-9: Polytomella F-ATP synthase associated subunit 9, ATP synthase associated protein ASA1, ... | | Authors: | Murphy, B.J, Klusch, N, Yildiz, O, Kuhlbrandt, W. | | Deposit date: | 2019-04-12 | | Release date: | 2019-07-03 | | Last modified: | 2024-10-23 | | Method: | ELECTRON MICROSCOPY (3.08 Å) | | Cite: | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364, 2019
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6Q45
 | | F1-ATPase from Fusobacterium nucleatum | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ATP synthase epsilon chain, ... | | Authors: | Petri, J, Nakatani, Y, Montgomery, M.G, Ferguson, S.A, Aragao, D, Leslie, A.G.W, Heikal, A, Walker, J.E, Cook, G.M. | | Deposit date: | 2018-12-05 | | Release date: | 2019-07-10 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (3.6 Å) | | Cite: | Structure of F1-ATPase from the obligate anaerobe Fusobacterium nucleatum.
Open Biology, 9, 2019
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5LQY
 | | Structure of F-ATPase from Pichia angusta, in state2 | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ATP synthase OSCP subunit, ... | | Authors: | Vinothkumar, K.R, Montgomery, M.G, Liu, S, Walker, J.E. | | Deposit date: | 2016-08-17 | | Release date: | 2016-11-16 | | Last modified: | 2024-05-15 | | Method: | ELECTRON MICROSCOPY (7.8 Å) | | Cite: | Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
Proc. Natl. Acad. Sci. U.S.A., 113, 2016
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5LQX
 | | Structure of F-ATPase from Pichia angusta, state3 | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ATP synthase AAP1 subunit, ... | | Authors: | Vinothkumar, K.R, Montgomery, M.G, Liu, S, Walker, J.E. | | Deposit date: | 2016-08-17 | | Release date: | 2016-11-16 | | Last modified: | 2024-05-15 | | Method: | ELECTRON MICROSCOPY (7.9 Å) | | Cite: | Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
Proc. Natl. Acad. Sci. U.S.A., 113, 2016
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5LQZ
 | | Structure of F-ATPase from Pichia angusta, state1 | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ATP synthase OSCP subunit, ... | | Authors: | Vinothkumar, K.R, Montgomery, M.G, Liu, S, Walker, J.E. | | Deposit date: | 2016-08-17 | | Release date: | 2016-11-16 | | Last modified: | 2024-05-15 | | Method: | ELECTRON MICROSCOPY (7 Å) | | Cite: | Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
Proc. Natl. Acad. Sci. U.S.A., 113, 2016
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6RD6
 | | CryoEM structure of Polytomella F-ATP synthase, focussed refinement of upper peripheral stalk | | Descriptor: | ASA-2: Polytomella F-ATP synthase associated subunit 2, ATP synthase subunit alpha, Mitochondrial ATP synthase associated protein ASA4, ... | | Authors: | Murphy, B.J, Klusch, N, Yildiz, O, Kuhlbrandt, W. | | Deposit date: | 2019-04-12 | | Release date: | 2019-07-03 | | Last modified: | 2024-05-22 | | Method: | ELECTRON MICROSCOPY (2.75 Å) | | Cite: | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364, 2019
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3M4Y
 | | Structural characterization of the subunit A mutant P235A of the A-ATP synthase | | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ACETIC ACID, ... | | Authors: | Manimekalai, M.S, Balakrishna, A.M, Kumar, A, Priya, R, Biukovic, G, Jeyakanthan, J, Gruber, G. | | Deposit date: | 2010-03-12 | | Release date: | 2011-01-26 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (2.38 Å) | | Cite: | The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding.
J.Mol.Biol., 401, 2010
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3I72
 | | Structural characterization for the nucleotide binding ability of subunit A with SO4 of the A1AO ATP synthase | | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, A-TYPE ATP SYNTHASE CATALYTIC SUBUNIT A, ... | | Authors: | Manimekalai, S.M.S, Kumar, A, Balakrishna, A.M, Gruber, G. | | Deposit date: | 2009-07-07 | | Release date: | 2010-01-12 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (2.47 Å) | | Cite: | Nucleotide binding states of subunit A of the A-ATP synthase and the implication of P-loop switch in evolution.
J.Mol.Biol., 396, 2010
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