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5OGL

Structure of bacterial oligosaccharyltransferase PglB in complex with an acceptor peptide and an lipid-linked oligosaccharide analog

5OGL の概要
エントリーDOI10.2210/pdb5ogl/pdb
分子名称Undecaprenyl-diphosphooligosaccharide--protein glycotransferase, Substrate mimicking peptide, MANGANESE (II) ION, ... (6 entities in total)
機能のキーワードoligosaccharyltransferase, complex, protein n-glycosylation, bacteria, membrane protein
由来する生物種Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
詳細
細胞内の位置Cell inner membrane ; Multi- pass membrane protein : B9KDD4
タンパク質・核酸の鎖数2
化学式量合計84675.63
構造登録者
Napiorkowska, M.,Boilevin, J.,Sovdat, T.,Darbre, T.,Reymond, J.-L.,Aebi, M.,Locher, K.P. (登録日: 2017-07-13, 公開日: 2017-10-25, 最終更新日: 2024-01-17)
主引用文献Napiorkowska, M.,Boilevin, J.,Sovdat, T.,Darbre, T.,Reymond, J.L.,Aebi, M.,Locher, K.P.
Molecular basis of lipid-linked oligosaccharide recognition and processing by bacterial oligosaccharyltransferase.
Nat. Struct. Mol. Biol., 24:1100-1106, 2017
Cited by
PubMed Abstract: Oligosaccharyltransferase (OST) is a membrane-integral enzyme that catalyzes the transfer of glycans from lipid-linked oligosaccharides (LLOs) onto asparagine side chains, the first step in protein N-glycosylation. Here, we report the X-ray structure of a single-subunit OST, PglB from Campylobacter lari, trapped in an intermediate state bound to an acceptor peptide and a synthetic LLO analog. The structure reveals the role of the external loop EL5, present in all OST enzymes, in substrate recognition. Whereas the N-terminal half of EL5 binds LLO, the C-terminal half interacts with the acceptor peptide. The glycan moiety of LLO must thread under EL5 to access the active site. Reducing EL5 mobility decreases the catalytic rate of OST when full-size heptasaccharide LLO is provided, but not for a monosaccharide-containing LLO analog. Our results define the chemistry of a ternary complex state, assign functional roles to conserved OST motifs, and provide opportunities for glycoengineering by rational design of PglB.
PubMed: 29058712
DOI: 10.1038/nsmb.3491
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 5ogl
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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