+Open data
-Basic information
Entry | Database: PDB / ID: 2wpd | ||||||
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Title | The Mg.ADP inhibited state of the yeast F1c10 ATP synthase | ||||||
Components | (ATP SYNTHASE SUBUNIT ...) x 6 | ||||||
Keywords | HYDROLASE / ATP PHOSPHORYLASE (H+ TRANSPORTING) / ATP-BINDING / CENTRAL STALK / ATP SYNTHESIS / PHOSPHOPROTEIN / MEMBRANE PROTEIN / LIPID-BINDING / ION TRANSPORT / NUCLEOTIDE-BINDING / HYDROGEN ION TRANSPORT | ||||||
Function / homology | Function and homology information mitochondrial proton-transporting ATP synthase, central stalk / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) ...mitochondrial proton-transporting ATP synthase, central stalk / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / 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 / mitochondrial intermembrane space / mitochondrial inner membrane / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.432 Å | ||||||
Authors | Dautant, A. / Velours, J. / Giraud, M.-F. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2010 Title: Crystal Structure of the Mg.Adp-Inhibited State of the Yeast F1C10-ATP Synthase. Authors: Dautant, A. / Velours, J. / Giraud, M. #1: Journal: Science / Year: 1999 Title: Molecular Architecture of the Rotary Motor in ATP Synthase. Authors: Stock, D. / Leslie, A.G.W. / Walker, J.E. #2: Journal: Embo J. / Year: 2006 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.W. / Mueller, D.M. #3: Journal: J.Biol.Chem. / Year: 2009 Title: Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides. Authors: Kabaleeswaran, V. / Shen, H. / Symersky, J. / Walker, J.E. / Leslie, A.G.W. / Mueller, D.M. #4: Journal: Science / Year: 2005 Title: Structure of the Rotor Ring of F-Type Na+-ATPase from Ilyobacter Tartaricus. Authors: Meier, T. / Polzer, P. / Diederichs, K. / Welte, W. / Dimroth, P. #5: 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. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wpd.cif.gz | 656.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wpd.ent.gz | 524.8 KB | Display | PDB format |
PDBx/mmJSON format | 2wpd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wp/2wpd ftp://data.pdbj.org/pub/pdb/validation_reports/wp/2wpd | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
-ATP SYNTHASE SUBUNIT ... , 6 types, 19 molecules ABCDEFGHIJKLMNOPQRS
#1: Protein | Mass: 55007.402 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: P07251 #2: Protein | Mass: 51181.082 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A References: UniProt: P00830, H+-transporting two-sector ATPase #3: Protein | | Mass: 30657.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: P38077 #4: Protein | | Mass: 14565.385 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: Q12165 #5: Protein | | Mass: 6618.359 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-62 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: P21306 #6: Protein | Mass: 7762.375 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A References: UniProt: P61829, H+-transporting two-sector ATPase |
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-Non-polymers , 3 types, 10 molecules
#7: Chemical | #8: Chemical | ChemComp-MG / #9: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.72 Å3/Da / Density % sol: 66.67 % / Description: NONE |
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Crystal grow | pH: 7.5 Details: 0.1 M HEPES/HCL PH 7.5, 12% PEG MME 5000, 100 MM SODIUM CHLORIDE MIXED 1:1 WITH PROTEIN SOLUTION CONTAINING 0.64 MM DDM, 25 MM TRIS/HCL PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 ...Details: 0.1 M HEPES/HCL PH 7.5, 12% PEG MME 5000, 100 MM SODIUM CHLORIDE MIXED 1:1 WITH PROTEIN SOLUTION CONTAINING 0.64 MM DDM, 25 MM TRIS/HCL PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 0.02% SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.66 MM ADP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 4, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.43→39.8 Å / Num. obs: 84424 / % possible obs: 88.1 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Biso Wilson estimate: 85 Å2 / Rmerge(I) obs: 0.19 / Net I/σ(I): 4.3 |
Reflection shell | Resolution: 3.43→3.62 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.72 / Mean I/σ(I) obs: 2.3 / % possible all: 64.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 2HLD, 1YCE Resolution: 3.432→39.775 Å / SU ML: 0.67 / σ(F): 1.34 / Phase error: 32.75 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.8 Å / VDW probe radii: 0.8 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 28.559 Å2 / ksol: 0.281 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 108 Å2
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Refinement step | Cycle: LAST / Resolution: 3.432→39.775 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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