1uf9

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1uf9, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of TT1252 from Thermus thermophilus

Overview

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.

About this Structure

1UF9 is a Single protein structure of sequence from Thermus thermophilus with PO4 and ATP as ligands. Full crystallographic information is available from OCA.

Reference

ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8., Seto A, Murayama K, Toyama M, Ebihara A, Nakagawa N, Kuramitsu S, Shirouzu M, Yokoyama S, Proteins. 2005 Jan 1;58(1):235-42. PMID:15526298

Page seeded by OCA on Wed Nov 21 04:05:12 2007