2cjl
From Proteopedia
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| - | [[Image:2cjl.gif|left|200px]] | + | [[Image:2cjl.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES''' | + | {{Structure |
| + | |PDB= 2cjl |SIZE=350|CAPTION= <scene name='initialview01'>2cjl</scene>, resolution 1.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CJL is a [ | + | 2CJL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17010167 17010167] |
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | [[Category: plant | + | [[Category: plant enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:14 2008'' |
Revision as of 14:16, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Chitinase, with EC number 3.2.1.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES
Overview
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 & 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.
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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