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Structure paper

TitleThe transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
Journal, issue, pagesJ. Mol. Biol., Vol. 408, Page 736-754, Year 2011
Publish dateJun 7, 2010 (structure data deposition date)
AuthorsManimekalai, M.S. / Kumar, A. / Jeyakanthan, J. / Gruber, G.
External linksJ. Mol. Biol. / PubMed:21396943
MethodsX-ray diffraction
Resolution2.4 - 3.1 Å
Structure data

PDB-3nd8:
Structural characterization for the nucleotide binding ability of subunit A of the A1AO ATP synthase
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3nd9:
Structural characterization for the nucleotide binding ability of subunit A of the A1AO ATP synthase
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-3p20:
Crystal structure of vanadate bound subunit A of the A1AO ATP synthase
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-ACY:
ACETIC ACID

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-VO4:
VANADATE ION

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • pyrococcus horikoshii (archaea)
KeywordsHYDROLASE / ATP Binding

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