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DOI | 10.2210/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: 29058712DOI: 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) |
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