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8A0M

Capsular polysaccharide synthesis multienzyme in complex with capsular polymer fragment

8A0M の概要
エントリーDOI10.2210/pdb8a0m/pdb
分子名称Bcs3, MAGNESIUM ION, beta-D-ribosyl-(1->1)-D-ribitol-5-phosphate, ... (4 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4
化学式量合計554609.54
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 (3.6 Å)
構造検証レポート
Validation report summary of 8a0m
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2025-12-31に公開中

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