Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, Wierenga RK. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5842-7. PMID:10823940
