1U8X

CRYSTAL STRUCTURE OF GLVA FROM BACILLUS SUBTILIS, A METAL-REQUIRING, NAD-DEPENDENT 6-PHOSPHO-ALPHA-GLUCOSIDASE

Replaces:  1NRH

Summary for 1U8X

• Entry DOI: 10.2210/pdb1u8x/pdb
• Related: 1NRH
• Descriptor: Maltose-6'-phosphate glucosidase, 6-O-phosphono-alpha-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: structural genomics, psi, protein structure initiative, mcsg, glucosidase, nad-dependent, midwest center for structural genomics, hydrolase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 55062.83

Authors

Rajan, S.S.,Yang, X.,Collart, F.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2004-08-09, release date: 2004-08-24, Last modification date: 2024-11-20)

Primary citation

Rajan, S.S.,Yang, X.,Collart, F.,Yip, V.L.,Withers, S.G.,Varrot, A.,Thompson, J.,Davies, G.J.,Anderson, W.F.
Novel Catalytic Mechanism of Glycoside Hydrolysis Based on the Structure of an NAD(+)/Mn(2+)-Dependent Phospho-alpha-Glucosidase from Bacillus subtilis.
STRUCTURE, 12:1619-1629, 2004

PubMed Abstract: GlvA, a 6-phospho-alpha-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6'-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 A resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.

PubMed: 15341727
DOI: 10.1016/j.str.2004.06.020

Experimental method

X-RAY DIFFRACTION (2.05 Å)