1UF9

Crystal structure of TT1252 from Thermus thermophilus

Summary for 1UF9

• Entry DOI: 10.2210/pdb1uf9/pdb
• Descriptor: TT1252 protein, PHOSPHATE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: p-loop, nucleotide binding domain, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (By similarity): Q56416
• Total number of polymer chains: 3
• Total formula weight: 69181.61

Authors

Seto, A.,Murayama, K.,Toyama, M.,Ebihara, A.,Nakagawa, N.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-05-28, release date: 2003-11-28, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)