1e15: Difference between revisions

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[[Image:1e15.gif|left|200px]]
{{Seed}}
[[Image:1e15.png|left|200px]]


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{{STRUCTURE_1e15|  PDB=1e15  |  SCENE=  }}  
{{STRUCTURE_1e15|  PDB=1e15  |  SCENE=  }}  


'''CHITINASE B FROM SERRATIA MARCESCENS'''
===CHITINASE B FROM SERRATIA MARCESCENS===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10823940}}


==About this Structure==
==About this Structure==
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[[Category: Chitin degradation]]
[[Category: Chitin degradation]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:31:50 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:58:13 2008''

Revision as of 20:58, 30 June 2008

File:1e15.png

Template:STRUCTURE 1e15

CHITINASE B FROM SERRATIA MARCESCENS

Template:ABSTRACT PUBMED 10823940

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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