Crystal structure of A-type ATP synthase catalytic nucleotide-binding subunit A from Pyrococcus horikoshii reveals a novel domain related in the

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H+-transporting ATP synthase is a multi-subunit enzyme involved in the production of ATP, which isessential molecule for living organisms as a source of energy. Archaeal A-type ATPase (A-ATPase) is thought to actas a functional ATP synthase in Archaea and is thought to have chimeric properties of F-ATPase and V-ATPase.From the previous structural studies of F-ATPase, it is indicated that the major nucleotide-binding subunits α and βconsist of three domains. The catalytic nucleotide-binding subunit A of V/A-ATPase contains an insertion of about90 residues, which is absent from the F1-β subunit. Here we describe the first X-ray structure of the catalyticnucleotide-binding subunit A of the A1-ATPase determined at 2.55 Å resolution. A1-ATPase subunit A fromPyrococcus horikoshii consists of four domains. A novel domain, including a part of this insertion, corresponds to the“knob-like structure” observed in electron microscopy of A1-ATPase. Based on the structure, it is highly likely thatthis inserted domain is related to the peripheral stalk common to the A- and V-ATPases. The arrangement of thisinserted domain suggests that this region plays an important role in A-ATPase as well as in V-ATPase.
International Union of Crystallographyの論文