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- PDB-3zry: Rotor architecture in the F(1)-c(10)-ring complex of the yeast F-... -
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Basic information
Entry | Database: PDB / ID: 3zry | |||||||||
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Title | Rotor architecture in the F(1)-c(10)-ring complex of the yeast F-ATP synthase | |||||||||
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![]() | HYDROLASE / ATP-BINDING / F(1)-F(O)ATP SYNTHASE / MITOCHONDRIA / MOLECULAR MOTOR / CENTRAL STALK / MEMBRANE PROTEIN / C-RING | |||||||||
Function / homology | ![]() mitochondrial proton-transporting ATP synthase, central stalk / : / : / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / mitochondrial proton-transporting ATP synthase complex / proton motive force-driven ATP synthesis ...mitochondrial proton-transporting ATP synthase, central stalk / : / : / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / mitochondrial proton-transporting ATP synthase complex / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton motive force-driven mitochondrial 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 / mitochondrial intermembrane space / ADP binding / mitochondrial inner membrane / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Giraud, M.-F. / Dautant, A. | |||||||||
![]() | ![]() Title: Rotor Architecture in the Yeast and Bovine F(1)-C-Ring Complexes of F-ATP Synthase. Authors: Giraud, M.-F. / Paumard, P. / Sanchez, C. / Brethes, D. / Velours, J. / Dautant, A. #1: ![]() Title: Crystal Structure of the Mgadp-Inhibited State of the Yeast F1C10-ATP Synthase. Authors: Dautant, A. / Velours, J. / Giraud, M. #2: Journal: J.Bioenerg.Biomembr. / Year: 2009 Title: Hydrogenated and Fluorinated Surfactants Derived from Tris(Hydroxymethyl)-Acrylamidomethane Allow the Purification of a Highly Active Yeast F1-F0 ATP-Synthase with an Enhanced Stability. Authors: Talbot, J.-C. / Dautant, A. / Polidori, A. / Pucci, B. / Cohen-Bouhacina, T. / Maali, A. / Salin, B. / Brethes, D. / Velours, J. / Giraud, M.-F. #3: ![]() Title: Molecular Architecture of the Rotary Motor in ATP Synthase Authors: Stock, D. / Leslie, A.G.W. / Walker, J.E. #4: ![]() Title: Novel Features of the Rotary Catalytic Mechanism Revealed in the Structure of Yeast F1 ATPase Authors: Kabaleeswaran, V. / Puri, N. / Walker, J.E. / Leslie, A.G. / Mueller, D.M. | |||||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 0-STRANDED BARREL THIS IS REPRESENTED BY A 1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 148.8 KB | Display | |
Data in CIF | ![]() | 197.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xokS S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Noncrystallographic symmetry (NCS) | NCS domain:
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