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8A0C

Capsular polysaccharide synthesis multienzyme in complex with CMP

8A0C の概要
エントリーDOI10.2210/pdb8a0c/pdb
分子名称Bcs3, PHOSPHATE ION, GLYCEROL, ... (6 entities in total)
機能のキーワードbacterial capsule synthesis, biosynthetic protein
由来する生物種Haemophilus influenzae
タンパク質・核酸の鎖数2
化学式量合計276932.04
構造登録者
主引用文献Cifuente, J.O.,Schulze, J.,Bethe, A.,Di Domenico, V.,Litschko, C.,Budde, I.,Eidenberger, L.,Thiesler, H.,Ramon Roth, I.,Berger, M.,Claus, H.,D'Angelo, C.,Marina, A.,Gerardy-Schahn, R.,Schubert, M.,Guerin, M.E.,Fiebig, T.
A multi-enzyme machine polymerizes the Haemophilus influenzae type b capsule.
Nat.Chem.Biol., 19:865-877, 2023
Cited by
PubMed Abstract: Bacterial capsules have critical roles in host-pathogen interactions. They provide a protective envelope against host recognition, leading to immune evasion and bacterial survival. Here we define the capsule biosynthesis pathway of Haemophilus influenzae serotype b (Hib), a Gram-negative bacterium that causes severe infections in infants and children. Reconstitution of this pathway enabled the fermentation-free production of Hib vaccine antigens starting from widely available precursors and detailed characterization of the enzymatic machinery. The X-ray crystal structure of the capsule polymerase Bcs3 reveals a multi-enzyme machine adopting a basket-like shape that creates a protected environment for the synthesis of the complex Hib polymer. This architecture is commonly exploited for surface glycan synthesis by both Gram-negative and Gram-positive pathogens. Supported by biochemical studies and comprehensive 2D nuclear magnetic resonance, our data explain how the ribofuranosyltransferase CriT, the phosphatase CrpP, the ribitol-phosphate transferase CroT and a polymer-binding domain function as a unique multi-enzyme assembly.
PubMed: 37277468
DOI: 10.1038/s41589-023-01324-3
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 8a0c
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-18に公開中

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