2005年
Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion
Biochemistry
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- ,
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- 巻
- 44
- 号
- 4
- 開始ページ
- 1136
- 終了ページ
- 1144
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1021/bi0484522
- 出版者・発行元
- AMER CHEMICAL SOC
Pyruvate phosphate dikinase (PPDK) reversibly catalyzes the conversion of ATP, phosphate, and pyruvate into AMP, pyrophosphate, and phosphoenolpyruvate (PEP), respectively. Since the nucleotide binding site (in the N-terminal domain) and the pyruvate/PEP binding site (in the C-terminal domain) are separated by similar to45 Angstrom, it has been proposed that an intermediary domain, called the central domain, swivels between these remote domains to transfer the phosphate. However, no direct structural evidence for the swiveling central domain has been found. In this study, the crystal structures of maize PPDK with and without PEP have been determined at 2.3 Angstrom resolution. These structures revealed that the central domain is located near the pyruvate/PEP binding C-terminal domain, in contrast to the PPDK from Clostridium symbiosum, wherein the central domain is located near the nucleotide-binding N-terminal domain. Structural comparisons between the maize and C. symbiosum PPDKs demonstrated that the swiveling motion of the central domain consists of a rotation of at least 92degrees and a translation of 0.5 Angstrom. By comparing the maize PPDK structures with and without PEP, we have elucidated the mode of binding of PEP to the C-terminal domain and the induced conformational changes in the central domain.
- リンク情報
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- DOI
- https://doi.org/10.1021/bi0484522
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000226594800006&DestApp=WOS_CPL
- URL
- http://www.scopus.com/inward/record.url?eid=2-s2.0-13444291928&partnerID=MN8TOARS
- ID情報
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- DOI : 10.1021/bi0484522
- ISSN : 0006-2960
- ORCIDのPut Code : 58433939
- SCOPUS ID : 13444291928
- Web of Science ID : WOS:000226594800006