Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli

DOIResolve DOI: http://doi.org/10.1110/ps.0227803
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TypeArticle
Volume12
Issue2
Pages327336; # of pages: 10
Subjectbiosynthesis; Escherichia coli; Filtration; Human; pha
AbstractCoenzyme 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
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
NoteEnglishJournal-Article2003110512538896
Peer reviewedNo
NRC number46177
NPARC number3539984
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Record identifier5d024722-ca7a-4fe9-9931-7a0dd192be93
Record created2009-03-01
Record modified2016-05-09
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