1UU6

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

1UU6 の概要

• エントリーDOI: 10.2210/pdb1uu6/pdb
• 関連するPDBエントリー: 1OLR 1UU4 1UU5 1W2U
• 関連するBIRD辞書のPRD_ID: PRD_900011
• 分子名称: ENDO-BETA-1,4-GLUCANASE, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: hydrolase, cellulase, cellulose degradation, endoglucanase, glycosyl hydrolase, gh family 12, humicola grisea cel12a, ligand complex
• 由来する生物種: HUMICOLA GRISEA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26749.39

構造登録者

Berglund, G.I.,Shaw, A.,Stahlberg, J.,Kenne, L.,Driguez, T.H.,Mitchinson, C.,Sandgren, M. (登録日: 2003-12-15, 公開日: 2004-09-16, 最終更新日: 2020-07-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.4 Å)