2cjl: Difference between revisions

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[[Image:2cjl.gif|left|200px]]
{{Seed}}
[[Image:2cjl.png|left|200px]]


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{{STRUCTURE_2cjl|  PDB=2cjl  |  SCENE=  }}  
{{STRUCTURE_2cjl|  PDB=2cjl  |  SCENE=  }}  


'''CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES'''
===CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES===




==Overview==
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We describe the cloning, overexpression, purification, characterization and crystal structure of chitinase G, a single-domain family 19 chitinase from the Gram-positive bacterium Streptomyces coelicolor A3(2). Although chitinase G was not capable of releasing 4-methylumbelliferyl from artificial chitooligosaccharide substrates, it was capable of degrading longer chitooligosaccharides at rates similar to those observed for other chitinases. The enzyme was also capable of degrading a colored colloidal chitin substrate (carboxymethyl-chitin-remazol-brilliant violet) and a small, presumably amorphous, subfraction of alpha-chitin and beta-chitin, but was not capable of degrading crystalline chitin completely. The crystal structures of chitinase G and a related Streptomyces chitinase, chitinase C [Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T &amp; Nonaka T (2006) J Mol Biol358, 472-484], showed that these bacterial family 19 chitinases lack several loops that extend the substrate-binding grooves in family 19 chitinases from plants. In accordance with these structural features, detailed analysis of the degradation of chitooligosaccharides by chitinase G showed that the enzyme has only four subsites (- 2 to + 2), as opposed to six (- 3 to + 3) for plant enzymes. The most prominent structural difference leading to reduced size of the substrate-binding groove is the deletion of a 13-residue loop between the two putatively catalytic glutamates. The importance of these two residues for catalysis was confirmed by a site-directed mutagenesis study.
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{{ABSTRACT_PUBMED_17010167}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Plant enzyme]]
[[Category: Plant enzyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:17:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:34:10 2008''

Revision as of 20:34, 27 July 2008

File:2cjl.png

Template:STRUCTURE 2cjl

CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES

Template:ABSTRACT PUBMED 17010167

About this Structure

2CJL is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.

Reference

Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes., Hoell IA, Dalhus B, Heggset EB, Aspmo SI, Eijsink VG, FEBS J. 2006 Nov;273(21):4889-900. Epub 2006 Sep 28. PMID:17010167

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