1w2u | pdb_00001w2u
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X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED THIO CELLOTETRAOSE
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
1W2U is a [Single protein] structure of sequence from [Humicola grisea] with SO4 and PG4 as [ligands]. Active as [[1]], with EC number [3.2.1.4]. 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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