論文

査読有り
2005年

Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion

Biochemistry
  • Nakanishi, T.
  • ,
  • Nakatsu, T.
  • ,
  • Matsuoka, M.
  • ,
  • Sakata, K.
  • ,
  • Kato, H.

44
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
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
  • DOI : 10.1021/bi0484522
  • ISSN : 0006-2960
  • ORCIDのPut Code : 58433939
  • SCOPUS ID : 13444291928
  • Web of Science ID : WOS:000226594800006

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