1uu4
From Proteopedia
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Revision as of 14:06, 30 October 2007
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X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH CELLOBIOSE
Overview
As part of an ongoing enzyme discovery program to investigate the, properties and catalytic mechanism of glycoside hydrolase family 12 (GH, 12) endoglucanases, a GH family that contains several cellulases that are, of interest in industrial applications, we have solved four new crystal, structures of wild-type Humicola grisea Cel12A in complexes formed by, soaking with cellobiose, cellotetraose, cellopentaose, and a thio-linked, cellotetraose derivative (G2SG2). These complex structures allow mapping, of the non-covalent interactions between the enzyme and the glucosyl chain, bound in subsites -4 to +2 of the enzyme, and shed light on the mechanism, and function of GH 12 cellulases. The unhydrolysed cellopentaose and the, G2SG2 cello-oligomers span the active site of the catalytically ... [(full description)]
About this Structure
1UU4 is a [Single protein] structure of sequence from [Humicola grisea] with PG4 as [ligand]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A., Sandgren M, Berglund GI, Shaw A, Stahlberg J, Kenne L, Desmet T, Mitchinson C, J Mol Biol. 2004 Oct 1;342(5):1505-17. PMID:15364577
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