論文

査読有り
2013年1月

Crystallographic and NMR Evidence for Flexibility in Oligosaccharyltransferases and Its Catalytic Significance

STRUCTURE
  • James Nyirenda
  • ,
  • Shunsuke Matsumoto
  • ,
  • Takashi Saitoh
  • ,
  • Nobuo Maita
  • ,
  • Nobuo N. Noda
  • ,
  • Fuyuhiko Inagaki
  • ,
  • Daisuke Kohda

21
1
開始ページ
32
終了ページ
41
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.str.2012.10.011
出版者・発行元
CELL PRESS

Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins. It possesses a binding pocket that recognizes Ser and Thr residues at the +2 position in the N-glycosylation consensus, Asn-X-Ser/Thr. We determined the crystal structures of the C-terminal globular domains of the catalytic subunits of two archaeal OSTs. A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects. We characterized its dynamic properties in solution by N-15 NMR relaxation analyses. Intriguingly, the mobile region contains the +2 Ser/Thr-binding pocket. In agreement, the flexibility restriction forced by an engineered disulfide cross-link abolished the enzymatic activity, and its cleavage fully restored activity. These results suggest the necessity of multiple conformational states in the reaction. The dynamic nature of the Ser/Thr pocket could facilitate the efficient scanning of N-glycosylation sequons along nascent polypeptide chains.

Web of Science ® 被引用回数 : 21

リンク情報
DOI
https://doi.org/10.1016/j.str.2012.10.011
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/23177926
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000313383400007&DestApp=WOS_CPL

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