1n3b

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spinqualitylabelsall models 1n3b, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Dephosphocoenzyme A kinase from Escherichia coli

Overview

Coenzyme A (CoA) is an essential cofactor used in a wide variety of, biochemical pathways. The final step in the biosynthesis of CoA is, catalyzed by dephosphocoenzyme A kinase (DPCK, E.C. 2.7.1.24). Here we, report the crystal structure of DPCK from Escherichia coli at 1.8 A, resolution. This enzyme forms a tightly packed trimer in its crystal, state, in contrast to its observed monomeric structure in solution and to, the monomeric, homologous DPCK structure from Haemophilus influenzae. We, have confirmed the existence of the trimeric form of the enzyme in, solution using gel filtration chromatography measurements. Dephospho-CoA, kinase is structurally similar to many nucleoside kinases and other, P-loop-containing nucleotide triphosphate hydrolases, despite having, negligible sequence similarity to these enzymes. Each monomer consists of, five parallel beta-strands flanked by alpha-helices, with an ATP-binding, site formed by a P-loop motif. Orthologs of the E. coli DPCK sequence, exist in a wide range of organisms, including humans. Multiple alignment, of orthologous DPCK sequences reveals a set of highly conserved residues, in the vicinity of the nucleotide/CoA binding site.

About this Structure

1N3B is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Active as Dephospho-CoA kinase, with EC number 2.7.1.24 Full crystallographic information is available from OCA.

Reference

Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli., O'Toole N, Barbosa JA, Li Y, Hung LW, Matte A, Cygler M, Protein Sci. 2003 Feb;12(2):327-36. PMID:12538896

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