1obb

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spinqualitylabelsall models 1obb, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ALPHA-GLUCOSIDASE A, AGLA, FROM THERMOTOGA MARITIMA IN COMPLEX WITH MALTOSE AND NAD+

Overview

Glycoside hydrolase family 4 represents an unusual group of glucosidases, with a requirement for NAD+, divalent metal cations, and reducing, conditions. The family is also unique in its inclusion of both alpha- and, beta-specific enzymes. The alpha-glucosidase A, AglA, from Thermotoga, maritima is a typical glycoside hydrolase family 4 enzyme, requiring NAD+, and Mn2+ as well as strongly reducing conditions for activity. Here we, present the crystal structure of the protein complexed with NAD+ and, maltose, refined at a resolution of 1.9 A. The NAD+ is bound to a typical, Rossman fold NAD+-binding site, and the nicotinamide moiety is localized, close to the maltose substrate. Within the active site the conserved, Cys-174 and surrounding histidines are positioned to play a role in the, ... [(full description)]

About this Structure

1OBB is a [Single protein] structure of sequence from [Thermotoga maritima] with MAL and NAD as [ligands]. Active as [[1]], with EC number [3.2.1.20]. Full crystallographic information is available from [OCA].

Reference

Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases., Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N, J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. PMID:12588867

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