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Structure paper

TitleEngineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 67, Page 1485-1491, Year 2011
Publish dateJun 9, 2011 (structure data deposition date)
AuthorsTadwal, V.S. / Manimekalai, M.S. / Gruber, G.
External linksActa Crystallogr. ,Sect. F / PubMed:22139149
MethodsX-ray diffraction
Resolution2.53 - 2.62 Å
Structure data

PDB-3sdz:
Structural characterization of the subunit A mutant F427W of the A-ATP synthase from Pyrococcus horikoshii
Method: X-RAY DIFFRACTION / Resolution: 2.53 Å

PDB-3se0:
Structural characterization of the subunit A mutant F508W of the A-ATP synthase from Pyrococcus horikoshii
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

Chemicals

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

ChemComp-ACY:
ACETIC ACID

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

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • pyrococcus horikoshii (archaea)
KeywordsHYDROLASE / A-Type ATP synthase / Adenine-binding pocket / Phenylalanine mutant

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