1UP6

Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate

Summary for 1UP6

• Entry DOI: 10.2210/pdb1up6/pdb
• Related: 1UP4 1UP7
• Descriptor: 6-PHOSPHO-BETA-GLUCOSIDASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, MANGANESE (II) ION, ... (6 entities in total)
• Functional Keywords: hydrolase, 6-phospho-beta-glucosidase, family4 hydrolase, nad dependent
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 8
• Total formula weight: 388450.42

Authors

Varrot, A.,Yip, V.L.,Withers, S.G.,Davies, G.J. (deposition date: 2003-09-29, release date: 2004-08-02, Last modification date: 2024-10-09)

Primary citation

Yip, V.L.,Varrot, A.,Davies, G.J.,Rajan, S.S.,Yang, X.,Thompson, J.,Anderson, W.F.,Withers, S.G.
An Unusual Mechanism of Glycoside Hydrolysis Involving Redox and Elimination Steps by a Family 4 Beta-Glycosidase from Thermotoga Maritima.
J.Am.Chem.Soc., 126:8354-, 2004

PubMed Abstract: Among the numerous well-characterized families of glycosidases, family 4 appears to be the anomaly, requiring both catalytic NAD+ and a divalent metal for activity. The unusual cofactor requirement prompted the proposal of a mechanism involving key NAD+-mediated redox steps as well as elimination of the glycosidic oxygen. Primary kinetic isotope effects for the 2- and 3-deutero substrate analogues, isotopic exchange with solvent, and structural analysis of a 6-phospho-beta-glucosidase, BglT (E.C. 3.2.1.6), provided evidence in support of the proposed mechanism, which has striking resemblances to that of the sugar dehydratases. Furthermore, analysis of the stereochemical outcome indicated that family 4 enzymes are retaining glycosidases.

PubMed: 15237973
DOI: 10.1021/JA047632W

Experimental method

X-RAY DIFFRACTION (2.55 Å)