5I1T
2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (SpoIID) from Clostridium difficile in Complex with Triacetylchitotriose
5I1T の概要
エントリーDOI | 10.2210/pdb5i1t/pdb |
関連するBIRD辞書のPRD_ID | PRD_900017 |
分子名称 | Stage II sporulation protein D, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (7 entities in total) |
機能のキーワード | spoiid, triacetylchitotriose, structural genomics, center for structural genomics of infectious diseases, csgid, hydrolase |
由来する生物種 | Peptoclostridium difficile (strain 630) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 38917.38 |
構造登録者 | Nocadello, S.,Minasov, G.,Shuvalova, L.,Dubrovska, I.,Grimshaw, S.,Kwon, K.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2016-02-05, 公開日: 2016-05-25, 最終更新日: 2023-09-27) |
主引用文献 | Nocadello, S.,Minasov, G.,Shuvalova, L.S.,Dubrovska, I.,Sabini, E.,Anderson, W.F. Crystal Structures of the SpoIID Lytic Transglycosylases Essential for Bacterial Sporulation. J.Biol.Chem., 291:14915-14926, 2016 Cited by PubMed Abstract: Bacterial spores are the most resistant form of life known on Earth and represent a serious problem for (i) bioterrorism attack, (ii) horizontal transmission of microbial pathogens in the community, and (iii) persistence in patients and in a nosocomial environment. Stage II sporulation protein D (SpoIID) is a lytic transglycosylase (LT) essential for sporulation. The LT superfamily is a potential drug target because it is active in essential bacterial processes involving the peptidoglycan, which is unique to bacteria. However, the absence of structural information for the sporulation-specific LT enzymes has hindered mechanistic understanding of SpoIID. Here, we report the first crystal structures with and without ligands of the SpoIID family from two community relevant spore-forming pathogens, Bacillus anthracis and Clostridium difficile. The structures allow us to visualize the overall architecture, characterize the substrate recognition model, identify critical residues, and provide the structural basis for catalysis by this new family of enzymes. PubMed: 27226615DOI: 10.1074/jbc.M116.729749 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 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
