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

被引:10
作者
Seto, A
Murayama, K
Toyama, M
Ebihara, A
Nakagawa, N
Kuramitsu, S
Shirouzu, M
Yokoyama, S
机构
[1] RIKEN, Genom Sci Ctr, Yokohama, Kanagawa 2300045, Japan
[2] Osaka Univ, Grad Sch Sci, Dept Biol, Osaka, Japan
[3] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Tokyo 113, Japan
关键词
kinase; ATP binding; structural change; crystal structure;
D O I
10.1002/prot.20276
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom. 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. (C) 2004 Wiley-Liss, Inc.
引用
收藏
页码:235 / 242
页数:8
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