8A0C
Capsular polysaccharide synthesis multienzyme in complex with CMP
8A0C の概要
エントリーDOI | 10.2210/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 | 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.,DAngelo, C.,Marina, A.,Gerardy-Schahn, R.,Schubert, M.,Guerin, M.E.,Fiebig, T. (登録日: 2022-05-27, 公開日: 2023-04-26, 最終更新日: 2024-05-01) |
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: 37277468DOI: 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
検証レポート(詳細版)
をダウンロード
