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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
| 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)
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Submitter: 渡邉 信久
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