1e15
From Proteopedia
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CHITINASE B FROM SERRATIA MARCESCENS
Overview
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.
About this Structure
1E15 is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.
Reference
Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution., van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, Wierenga RK, Proc Natl Acad Sci U S A. 2000 May 23;97(11):5842-7. PMID:10823940
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