Crystal Structure of Dephospho-Coenzyme A Kinase from Haemophilus Influenzae

Published

November 1, 2001

Author(s)

G Obmolova, A Teplyakov, N Bonander, E Eisenstein, A J. Howard, G L. Gilliland

Abstract

phospho-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 determined at 2.0- resolution in complex with ATP. The protein molecule consists of three domains: the canonical nucleotide binding domain with a five-stranded parallel b-sheet, the substrate-binding a-helical domain, and the lid domain formed by a pair of a-helices. The overall topology of the protein resembles the structures of nucleotide kinases. ATP binds inthe 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 involved in substrate binding and catalysis have been identified. The structure analysis suggests large domain movements during the catalytic cycle.

Citation

Journal of Structural Biology

Volume

136

Issue

No. 2

Pub Type

Journals

Keywords

CoA Synthesis, kinase, nucleotide binding fold, structural genomics

Citation

Obmolova, G. , Teplyakov, A. , Bonander, N. , Eisenstein, E. , Howard, A. and Gilliland, G. (2001), Crystal Structure of Dephospho-Coenzyme A Kinase from Haemophilus Influenzae, Journal of Structural Biology (Accessed October 24, 2025)