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ATP‐induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8
Author(s) -
Seto Azusa,
Murayama Kazutaka,
Toyama Mitsutoshi,
Ebihara Akio,
Nakagawa Noriko,
Kuramitsu Seiki,
Shirouzu Mikako,
Yokoyama Shigeyuki
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20276
Subject(s) - thermus thermophilus , biology , adenosine triphosphate , protein structure , histidine kinase , phosphorylation , biochemistry , chemistry , crystallography , stereochemistry , amino acid , escherichia coli , histidine , gene
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. Proteins 2005. © 2004 Wiley‐Liss, Inc.