Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.05
Classification:HYDROLASE
Release Date:2004-08-24
Deposition Date:2004-08-09
Revision Date:2008-04-30#2011-07-13
Molecular Weight:55062.83
Macromolecule Type:Protein
Residue Count:472
Atom Site Count:3510
DOI:10.2210/pdb1u8x/pdb
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.
Resolution:2.05
Classification:HYDROLASE
Release Date:2004-08-24
Deposition Date:2004-08-09
Revision Date:2008-04-30#2011-07-13
Molecular Weight:55062.83
Macromolecule Type:Protein
Residue Count:472
Atom Site Count:3510
DOI:10.2210/pdb1u8x/pdb
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.
| Date made available | 2004 |
|---|---|
| Publisher | RCSB-PDB |