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Yorodumi- PDB-2rq7: Solution structure of the epsilon subunit chimera combining the N... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2rq7 | ||||||
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Title | Solution structure of the epsilon subunit chimera combining the N-terminal beta-sandwich domain from T. Elongatus bp-1 f1 and the C-terminal alpha-helical domain from spinach chloroplast F1 | ||||||
Components | ATP synthase epsilon chain,ATP synthase epsilon chain, chloroplastic | ||||||
Keywords | HYDROLASE / ATP SYNTHASE / F1FO ATP SYNTHASE / F1-ATPASE / EPSILON SUBUNIT / CHLOROPLAST / ATP SYNTHESIS / CF1 / HYDROGEN ION TRANSPORT / ION TRANSPORT / MEMBRANE / THYLAKOID / TRANSPORT / PLASTID / CF(1) | ||||||
Function / homology | Function and homology information plasma membrane-derived thylakoid membrane / proton motive force-driven ATP synthesis / chloroplast thylakoid membrane / proton-transporting ATP synthase complex, catalytic core F(1) / proton-transporting ATP synthase activity, rotational mechanism / ATP binding Similarity search - Function | ||||||
Biological species | Thermosynechococcus elongatus (bacteria) Spinacia oleracea (spinach) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Yagi, H. / Konno, H. / Murakami-Fuse, T. / Oroguchi, H. / Akutsu, T. / Ikeguchi, M. / Hisabori, T. | ||||||
Citation | Journal: Biochem.J. / Year: 2010 Title: Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms. Authors: Yagi, H. / Konno, H. / Murakami-Fuse, T. / Isu, A. / Oroguchi, T. / Akutsu, H. / Ikeguchi, M. / Hisabori, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rq7.cif.gz | 926.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rq7.ent.gz | 792.3 KB | Display | PDB format |
PDBx/mmJSON format | 2rq7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/2rq7 ftp://data.pdbj.org/pub/pdb/validation_reports/rq/2rq7 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14602.535 Da / Num. of mol.: 1 / Mutation: K109A Source method: isolated from a genetically manipulated source Details: The fusion protein of beta-sandwich domain (residues 1-88) from T. Elongatus bp-1 F1 and alpha-helical domain (residues 89-134) from spinach chloroplast F1 Source: (gene. exp.) Thermosynechococcus elongatus (strain BP-1) (bacteria), (gene. exp.) Spinacia oleracea (spinach) Strain: BP-1 / Gene: atpC, atpE, tlr0526, atpE / Production host: Escherichia coli (E. coli) / References: UniProt: Q8DLG7, UniProt: P00833 |
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Sequence details | THE FUSION PROTEIN OF BETA-SANDWICH DOMAIN (RESIDUES 1-88) FROM T. ELONGATUS BP-1 F1 AND ALPHA- ...THE FUSION PROTEIN OF BETA-SANDWICH DOMAIN (RESIDUES 1-88) FROM T. ELONGATUS BP-1 F1 AND ALPHA-HELICAL DOMAIN (RESIDUES 89-134) FROM SPINACH CHLOROPLAS |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.0 mM [U-99% 15N] ATP SYNTHASE EPSILON CHAIN-1, 1.0 mM [U-99% 13C; U-99% 15N] ATP SYNTHASE EPSILON CHAIN-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 6.8 / Pressure: AMBIENT / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |