2cjl: Difference between revisions
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[[Image:2cjl.gif|left|200px]]<br /><applet load="2cjl" size=" | [[Image:2cjl.gif|left|200px]]<br /><applet load="2cjl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2cjl, resolution 1.50Å" /> | caption="2cjl, resolution 1.50Å" /> | ||
'''CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES'''<br /> | '''CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2CJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Zn Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 2CJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: plant enzymes]] | [[Category: plant enzymes]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:36:08 2008'' | ||
Revision as of 11:36, 3 February 2008
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CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES
OverviewOverview
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 StructureAbout this Structure
2CJL is a Single protein structure of sequence from Streptomyces coelicolor with as ligand. Active as Chitinase, with EC number 3.2.1.14 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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