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Structure paper

TitleThe critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding.
Journal, issue, pagesJ. Mol. Biol., Vol. 401, Page 892-905, Year 2010
Publish dateMar 12, 2010 (structure data deposition date)
AuthorsKumar, A. / Manimekalai, M.S. / Balakrishna, A.M. / Priya, R. / Biukovic, G. / Jeyakanthan, J. / Gruber, G.
External linksJ. Mol. Biol. / PubMed:20615420
MethodsX-ray diffraction
Resolution2.35 - 2.38 Å
Structure data

PDB-3m4y:
Structural characterization of the subunit A mutant P235A of the A-ATP synthase
Method: X-RAY DIFFRACTION / Resolution: 2.38 Å

PDB-3mfy:
Structural characterization of the subunit A mutant F236A of the A-ATP synthase from Pyrococcus horikoshii
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

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

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

ChemComp-ACY:
ACETIC ACID

ChemComp-HOH:
WATER

Source
  • pyrococcus horikoshii ot3 (archaea)
  • pyrococcus horikoshii (archaea)
KeywordsHYDROLASE / ATP synthesis / ATP-binding / Autocatalytic cleavage / Hydrogen ion transport / Intron homing / Ion transport / Nuclease / Nucleotide-binding / Transport / A-Type ATP synthase / P loop / Phenylalanine mutant

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