ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8

Azusa Seto, Kazutaka Murayama, Mitsutoshi Toyama, Akio Ebihara, Noriko Nakagawa, Seiki Kuramitsu, Mikako Shirouzu, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Dephosphocoenzyme A kinase (DCK) catalyzes phosphorylation in the final step of coenzyme A (CoA) biosynthesis. In this phosphorylation process, domain movements play a very important role. To reveal the structural changes induced by ligand binding, we determined the crystal structure of DCK from Thermus thermophilus HB8 by the multiwavelength anomalous dispersion method at 2.8 Å. The crystal structure includes three independent protein molecules in the asymmetric unit: One is a liganded form and the others are unliganded. The topology shows a canonical nucleotide-binding protein possessing the P-loop motif. A structure homology search by DALI revealed the similarity of the DCKs from T. thermophilus HB8, Haemophilus influenzae, and Escherichia coli. Structural comparisons between the liganded and unliganded forms of DCK from T. thermophilus HB8 indicated domain movements induced by adenosine triphosphate (ATP) binding. For the domain movements, proline residues confer flexibility at the domain linkages. In particular, Pro91 plays an important role in moving the CoA domain.

Original languageEnglish
Pages (from-to)235-242
Number of pages8
JournalProteins: Structure, Function and Genetics
Issue number1
Publication statusPublished - 2005 Jan 1
Externally publishedYes


  • ATP binding
  • Crystal structure
  • Kinase
  • Structural change

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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