1e15
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e15 OCA], [http://www.ebi.ac.uk/pdbsum/1e15 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e15 RCSB]</span> | ||
}} | }} | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:55 2008'' |
Revision as of 16:52, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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