Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution.

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.

authors

van Aalten DM,Synstad B,Brurberg MB,Hough E,Riise BW,Eijsink VG,Wierenga RK

doi

10.1073/pnas.97.11.5842

keywords:

subject

Has Abstract

pub_date

2000-05-23 00:00:00

pages

5842-7

issue

11

eissn

0027-8424

issn

1091-6490

pii

97/11/5842

journal_volume

97

pub_type

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