2cjl
From Proteopedia
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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, ... [(full description)]
About this Structure
2CJL is a [Single protein] structure of sequence from [Streptomyces coelicolor] with ZN as [ligand]. Active as [[1]], with EC number [3.2.1.14]. 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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