1E15

Chitinase B from Serratia Marcescens

1E15 の概要

• エントリーDOI: 10.2210/pdb1e15/pdb
• 関連するPDBエントリー: 1CTN
• 分子名称: CHITINASE B (2 entities in total)
• 機能のキーワード: hydrolase, chitin degradation
• 由来する生物種: SERRATIA MARCESCENS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 111036.02

構造登録者

Van Aalten, D.M.F.,Synstad, B.,Brurberg, M.B.,Hough, E.,Riise, B.W.,Eijsink, V.G.H.,Wierenga, R.K. (登録日: 2000-04-18, 公開日: 2000-08-18, 最終更新日: 2024-11-13)

主引用文献

Van Aalten, D.M.F.,Synstad, B.,Brurberg, M.B.,Hough, E.,Riise, B.W.,Eijsink, V.G.H.,Wierenga, R.K.
Structure of a Two-Domain Chitotriosidase from Serratia Marcescens at 1.9 Angstrom Resoltuion
Proc.Natl.Acad.Sci.USA, 97:5842-, 2000

PubMed Abstract: In this paper, we describe the structure of chitinase B from Serratia marcescens, which consists of a catalytic domain with a TIM-barrel fold and a 49-residue C-terminal chitin-binding domain. This chitinase is the first structure of a bacterial exochitinase, and it represents one of only a few examples of a glycosyl hydrolase structure having interacting catalytic and substrate-binding domains. The chitin-binding domain has exposed aromatic residues that contribute to a 55-A long continuous aromatic stretch extending into the active site. Binding of chitin oligomers is blocked beyond the -3 subsite, which explains why the enzyme has chitotriosidase activity and degrades the chitin chain from the nonreducing end. Comparison of the chitinase B structure with that of chitinase A explains why these enzymes act synergistically in the degradation of chitin.

PubMed: 10823940
DOI: 10.1073/PNAS.97.11.5842

実験手法

X-RAY DIFFRACTION (1.9 Å)