1hdi

From Proteopedia

Revision as of 13:29, 30 October 2007

PIG MUSCLE 3-PHOSPHOGLYCERATE KINASE COMPLEXED WITH 3-PG AND MGADP.

Overview

3-phosphoglycerate kinase (PGK) is a typical kinase with two structural, domains. The domains each bind one of the two substrates, 3-phosphoglycerate (3-PG) and MgATP. For the phospho-transfer reaction to, take place the substrates must be brought closer by a hinge-bending domain, closure. Open and closed structures of the enzyme with different relative, domain positions have been determined from different species, but a, comprehensive description of this conformational transition is yet to be, attained. Crystals of pig muscle PGK in complex with MgADP and, 3-phosphoglycerate were grown under the conditions which have previously, resulted in crystals of the closed, catalytically competent conformation, of Trypanosoma brucei PGK. The X-ray structure of the pig muscle ternary, complex was ... [(full description)]

About this Structure

1HDI is a [Single protein] structure of sequence from [Sus scrofa] with MG, AMP and 3PG as [ligands]. Active as [Phosphoglycerate kinase], with EC number [2.7.2.3]. Structure known Active Sites: 3PG and AMP. Full crystallographic information is available from [OCA].

Reference

A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure., Szilagyi AN, Ghosh M, Garman E, Vas M, J Mol Biol. 2001 Feb 23;306(3):499-511. PMID:11178909

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