6EJK
Structure of a glycosyltransferase
6EJK の概要
| エントリーDOI | 10.2210/pdb6ejk/pdb |
| 関連するPDBエントリー | 6EJJ |
| 分子名称 | WlaC protein, 2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-glucopyranose, Uridine-Diphosphate-Methylene-N-acetyl-galactosamine, ... (4 entities in total) |
| 機能のキーワード | glycosyltransferase, transferase |
| 由来する生物種 | Campylobacter jejuni |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 89877.78 |
| 構造登録者 | Ramirez, A.S.,Boilevin, J.,Mehdipour, A.R.,Hummer, G.,Darbre, T.,Reymond, J.L.,Locher, K.P. (登録日: 2017-09-21, 公開日: 2018-02-07, 最終更新日: 2024-11-13) |
| 主引用文献 | Ramirez, A.S.,Boilevin, J.,Mehdipour, A.R.,Hummer, G.,Darbre, T.,Reymond, J.L.,Locher, K.P. Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase. Nat Commun, 9:445-445, 2018 Cited by PubMed Abstract: The membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Using an unknown counting mechanism, PglH catalyzes the transfer of exactly three α1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-α1,4-GalNAc-α1,3-Bac-α1-PP-undecaprenyl. Here, we present crystal structures of PglH in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analog and either UDP or synthetic, nonhydrolyzable UDP-CH-GalNAc. PglH contains an amphipathic helix ("ruler helix") that has a dual role of facilitating membrane attachment and glycan counting. The ruler helix contains three positively charged side chains that can bind the pyrophosphate group of the LLO substrate and thus limit the addition of GalNAc units to three. These results, combined with molecular dynamics simulations, provide the mechanism of glycan counting by PglH. PubMed: 29386647DOI: 10.1038/s41467-018-02880-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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