2V5C

Family 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structure

2V5C の概要

• エントリーDOI: 10.2210/pdb2v5c/pdb
• 関連するPDBエントリー: 2J62 2JH2 2V5D 2VUR
• 分子名称: O-GLCNACASE NAGJ, CALCIUM ION, CACODYLATE ION, ... (5 entities in total)
• 機能のキーワード: glycosidase, clostridium perfringens, gh84, gh84c, hydrolase, coiled coil, family 84 glycoside hydrolase, carbohydrate binding module
• 由来する生物種: CLOSTRIDIUM PERFRINGENS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 134268.66

構造登録者

Ficko-Blean, E.,Gregg, K.J.,Adams, J.J.,Hehemann, J.H.,Smith, S.J.,Czjzek, M.,Boraston, A.B. (登録日: 2008-10-02, 公開日: 2009-01-27, 最終更新日: 2024-05-08)

主引用文献

Ficko-Blean, E.,Gregg, K.J.,Adams, J.J.,Hehemann, J.H.,Smith, S.J.,Czjzek, M.,Boraston, A.B.
Portrait of an Enzyme: A Complete Structural Analysis of a Multi-Modular Beta-N-Acetylglucosaminidase from Clostridium Perfringens
J.Biol.Chem., 284:9876-, 2009

PubMed Abstract: Common features of the extracellular carbohydrate-active virulence factors involved in host-pathogen interactions are their large sizes and modular complexities. This has made them recalcitrant to structural analysis, and therefore our understanding of the significance of modularity in these important proteins is lagging. Clostridium perfringens is a prevalent human pathogen that harbors a wide array of large, extracellular carbohydrate-active enzymes and is an excellent and relevant model system to approach this problem. Here we describe the complete structure of C. perfringens GH84C (NagJ), a 1001-amino acid multimodular homolog of the C. perfringens micro-toxin, which was determined using a combination of small angle x-ray scattering and x-ray crystallography. The resulting structure reveals unprecedented insight into how catalysis, carbohydrate-specific adherence, and the formation of molecular complexes with other enzymes via an ultra-tight protein-protein interaction are spatially coordinated in an enzyme involved in a host-pathogen interaction.

PubMed: 19193644
DOI: 10.1074/JBC.M808954200

実験手法

X-RAY DIFFRACTION (2.1 Å)