1u8x

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1u8x, resolution 2.05Å

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

Overview

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.

About this Structure

1U8X is a Single protein structure of sequence from Bacillus subtilis with G6P, MN and NAD as ligands. This structure superseeds the now removed PDB entry 1NRH. Active as Maltose-6'-phosphate glucosidase, with EC number 3.2.1.122 Full crystallographic information is available from OCA.

Reference

Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis., Rajan SS, Yang X, Collart F, Yip VL, Withers SG, Varrot A, Thompson J, Davies GJ, Anderson WF, Structure. 2004 Sep;12(9):1619-29. PMID:15341727

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