1e15: Difference between revisions

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[[Image:1e15.~~gif~~|left|200px]]

[[Image:1e15.png|left|200px]]

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~~'''~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_10823940}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10823940 is the PubMed ID number.

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==About this Structure==

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[[Category: Chitin degradation]]

[[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''

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-[[Image:1e15.gif|left|200px]]
+{{Seed}}
+[[Image:1e15.png|left|200px]]
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 {{STRUCTURE_1e15|  PDB=1e15  |  SCENE=  }}
-'''CHITINASE B FROM SERRATIA MARCESCENS'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10823940}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10823940 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10823940}}
 ==About this Structure==
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 [[Category: Chitin degradation]]
 [[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''