1W2U

X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED THIO CELLOTETRAOSE

Summary for 1W2U

• Entry DOI: 10.2210/pdb1w2u/pdb
• Related: 1OLR 1UU5 1UU6
• Related PRD ID: PRD_900011
• Descriptor: ENDOGLUCANASE, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total)
• Functional Keywords: hydrolase, cellulase, cellulose degradation, endoglucanase, glycosyl hydrolase, gh family 12, humicola grisea cel12a, ligand complex
• Biological source: HUMICOLA GRISEA
• Total number of polymer chains: 1
• Total formula weight: 26845.45

Authors

Berglund, G.I.,Shaw, A.,Stahlberg, J.,Kenne, L.,Driguez, T.H.,Mitchinson, C.,Sandgren, M. (deposition date: 2004-07-08, release date: 2004-09-16, Last modification date: 2020-07-29)

Primary citation

Sandgren, M.,Berglund, G.I.,Shaw, A.,Stahlberg, J.,Kenne, L.,Desmet, T.,Mitchinson, C.
Crystal Complex Structures Reveal How Substrate is Bound in the -4 to the +2 Binding Sites of Humicola Grisea Cel12A
J.Mol.Biol., 342:1505-, 2004

PubMed Abstract: 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 active H.grisea Cel12A enzyme, with the pyranoside bound in subsite -1 displaying a S31 skew boat conformation. After soaking in cellotetraose, the cello-oligomer that is found bound in site -4 to -1 contains a beta-1,3-linkage between the two cellobiose units in the oligomer, which is believed to have been formed by a transglycosylation reaction that has occurred during the ligand soak of the protein crystals. The close fit of this ligand and the binding sites occupied suggest a novel mixed beta-glucanase activity for this enzyme.

PubMed: 15364577
DOI: 10.1016/J.JMB.2004.07.098

Experimental method

X-RAY DIFFRACTION (1.52 Å)