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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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Title: Crystal structure of A-type ATP synthase catalytic nucleotide-binding subunit A from Pyrococcus horikoshii reveals a novel domain related in the
Authors: Maegawa, Yuki Browse this author
Morita, Hazuki Browse this author
Iyaguchi, Daisuke Browse this author
Yao, Min Browse this author →KAKEN DB
Watanabe, Nobuhisa Browse this author
Tanaka, Isao Browse this author →KAKEN DB
Keywords: H+-transporting ATP synthase
A-ATPase
catalytic nucleotide-binding subunit A
archaea
X-ray crystallography
Issue Date: May-2006
Publisher: International Union of Crystallography
Journal Title: Acta Crystallographica Section D
Volume: 62
Issue: 5
Start Page: 483
End Page: 488
Publisher DOI: 10.1107/S0907444906006329
PMID: 16627940
Abstract: H+-transporting ATP synthase is a multi-subunit enzyme involved in the production of ATP, which is essential molecule for living organisms as a source of energy. Archaeal A-type ATPase (A-ATPase) is thought to act as 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 β consist of three domains. The catalytic nucleotide-binding subunit A of V/A-ATPase contains an insertion of about 90 residues, which is absent from the F1-β subunit. Here we describe the first X-ray structure of the catalytic nucleotide-binding subunit A of the A1-ATPase determined at 2.55 Å resolution. A1-ATPase subunit A from Pyrococcus 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 that this inserted domain is related to the peripheral stalk common to the A- and V-ATPases. The arrangement of this inserted domain suggests that this region plays an important role in A-ATPase as well as in V-ATPase.
Rights: Copyright © International Union of Crystallography
Type: article (author version)
URI: http://hdl.handle.net/2115/8534
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 渡邉 信久

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