1jjv

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Revision as of 16:12, 20 November 2007

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spinqualitylabelsall models 1jjv, resolution 2.Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

DEPHOSPHO-COA KINASE IN COMPLEX WITH ATP

Overview

Dephospho-coenzyme A kinase catalyzes the final step in CoA biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a, phosphate donor. The protein from Haemophilus influenzae was cloned and, expressed, and its crystal structure was determined at 2.0-A resolution in, complex with ATP. The protein molecule consists of three domains: the, canonical nucleotide-binding domain with a five-stranded parallel, beta-sheet, the substrate-binding alpha-helical domain, and the lid domain, formed by a pair of alpha-helices. The overall topology of the protein, resembles the structures of nucleotide kinases. ATP binds in the P-loop in, a manner observed in other kinases. The CoA-binding site is located at the, interface of all three domains. The double-pocket structure of the, substrate-binding site is unusual for nucleotide kinases. Amino acid, residues implicated in substrate binding and catalysis have been, identified. The structure analysis suggests large domain movements during, the catalytic cycle.

About this Structure

1JJV is a Single protein structure of sequence from Haemophilus influenzae with SO4, HG and ATP as ligands. Active as Dephospho-CoA kinase, with EC number 2.7.1.24 Full crystallographic information is available from OCA.

Reference

Crystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae., Obmolova G, Teplyakov A, Bonander N, Eisenstein E, Howard AJ, Gilliland GL, J Struct Biol. 2001 Nov;136(2):119-25. PMID:11886213

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