1UF9

Crystal structure of TT1252 from Thermus thermophilus

1UF9 の概要

• エントリーDOI: 10.2210/pdb1uf9/pdb
• 分子名称: TT1252 protein, PHOSPHATE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: p-loop, nucleotide binding domain, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm (By similarity): Q56416
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 69181.61

構造登録者

Seto, A.,Murayama, K.,Toyama, M.,Ebihara, A.,Nakagawa, N.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-05-28, 公開日: 2003-11-28, 最終更新日: 2024-10-30)

主引用文献

Seto, A.,Murayama, K.,Toyama, M.,Ebihara, A.,Nakagawa, N.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8
PROTEINS, 58:235-242, 2005

PubMed Abstract: 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 A. 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.

PubMed: 15526298
DOI: 10.1002/prot.20276

実験手法

X-RAY DIFFRACTION (2.8 Å)