1ygy

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1ygy, resolution 2.30Å

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Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis

Overview

Phosphoglycerate dehydrogenases exist in at least three different, structural motifs. The first D-3-phosphoglycerate dehydrogenase structure, to be determined was from Escherichia coli and is a tetramer composed of, identical subunits that contain three discernable structural domains. The, crystal structure of D-3-phosphoglycerate dehydrogenase from Mycobacterium, tuberculosis has been determined at 2.3 A. This enzyme represents a second, structural motif of the D-3-phosphoglycerate dehydrogenase family, one, that contains an extended C-terminal region. This structure is also a, tetramer of identical subunits, and the extended motif of 135 amino acids, exists as a fourth structural domain. This intervening domain exerts quite, a surprising characteristic to the structure by introducing significant, asymmetry in the tetramer. The asymmetric unit is composed of two, identical subunits that exist in two different conformations characterized, by rotation of approximately 180 degrees around a hinge connecting two of, the four domains. This asymmetric arrangement results in the formation of, two different and distinct domain interfaces between identical domains in, the asymmetric unit. As a result, the surface of the intervening domain, that is exposed to solvent in one subunit is turned inward in the other, subunit toward the center of the structure where it makes contact with, other structural elements. Significant asymmetry is also seen at the, subunit level where different conformations exist at the NAD-binding site, and the putative serine-binding site in the two unique subunits.

About this Structure

1YGY is a Single protein structure of sequence from Mycobacterium tuberculosis with TAR as ligand. Active as Phosphoglycerate dehydrogenase, with EC number 1.1.1.95 Full crystallographic information is available from OCA.

Reference

Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits., Dey S, Grant GA, Sacchettini JC, J Biol Chem. 2005 Apr 15;280(15):14892-9. Epub 2005 Jan 24. PMID:15668249

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