;Engineered 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.
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Acta Crystallogr.,Sect.F (2011)
Nucleotide binding states of subunit A of the A-ATP synthase and the implication of P-loop switch in evolution.
J.Mol.Biol. (2010)
;Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk.
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Acta Crystallogr.,Sect.D (2006)