1uf9

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{{Structure
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uf9 OCA], [http://www.ebi.ac.uk/pdbsum/1uf9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uf9 RCSB]</span>
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'''Crystal structure of TT1252 from Thermus thermophilus'''
'''Crystal structure of TT1252 from Thermus thermophilus'''
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[[Category: Toyama, M.]]
[[Category: Toyama, M.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: nucleotide binding domain]]
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[[Category: Nucleotide binding domain]]
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[[Category: p-loop]]
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[[Category: P-loop]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: Rsgi]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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Revision as of 08:08, 3 May 2008

Image:1uf9.jpg

Template:STRUCTURE 1uf9

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. 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 Sat May 3 11:08:36 2008

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