Structure of a Two-domain Chitotriosidase from Serratia Marcescens at 1.9-A Resolution

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2000 May 24

PMID 10823940

Citations 70

Authors

D M van Aalten

B Synstad

M B Brurberg

E Hough

B W Riise

V G Eijsink

R K Wierenga

Affiliations

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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.

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