1E15

Chitinase B from Serratia Marcescens

Summary for 1E15

• Entry DOI: 10.2210/pdb1e15/pdb
• Related: 1CTN
• Descriptor: CHITINASE B (2 entities in total)
• Functional Keywords: hydrolase, chitin degradation
• Biological source: SERRATIA MARCESCENS
• Total number of polymer chains: 2
• Total formula weight: 111036.02

Authors

Van Aalten, D.M.F.,Synstad, B.,Brurberg, M.B.,Hough, E.,Riise, B.W.,Eijsink, V.G.H.,Wierenga, R.K. (deposition date: 2000-04-18, release date: 2000-08-18, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)