2013年1月
Crystallographic and NMR Evidence for Flexibility in Oligosaccharyltransferases and Its Catalytic Significance
STRUCTURE
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- 巻
- 21
- 号
- 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
Web of Science ® の 関連論文(Related Records®)ビュー
- リンク情報
- ID情報
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- DOI : 10.1016/j.str.2012.10.011
- ISSN : 0969-2126
- PubMed ID : 23177926
- Web of Science ID : WOS:000313383400007