Document Detail


Structural basis of CoA recognition by the Pyrococcus single-domain CoA-binding proteins.
MedLine Citation:
PMID:  17342453     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The single-domain coenzyme A (CoA)-binding protein is conserved in bacteria, archaea, and a few eukaryal taxa. It consists of a Rossmann-fold domain, belonging to the FAD/NAD(P)-binding ;superfamily. The crystal structure of the Thermus thermophilus single-domain CoA-binding protein, TTHA1899, has been determined and it has been demonstrated, by isothermal titration calorimetry, that the protein interacts with CoA [Wada T. et al. Acta Crystallogr D Biol Crystallogr 59 (2003) 1213]. In the present study, we determined the crystal structures of an orthologous protein from the archaeon Pyrococcus horikoshii (PH1109), alone and complexed with CoA, at 1.65 A and 1.70 A resolutions, respectively, and that of P. furiosus protein (PF0725) in the CoA-bound form at 1.70 A. The CoA-bound structures are very similar to each other, revealing that the Pyrococcus proteins bind CoA in a 1:1 stoichiometry. Five loop-containing regions form the CoA-binding groove, to which the CoA molecule is docked. A comparison of the structures and the sequences of the Pyrococcus proteins with those of the T. theromphilus orthologue TTHA1899 indicated that archaeal and bacterial single-domain CoA-binding proteins share the same CoA-binding mode. Nevertheless, many of the peripheral residues involved in the hydrogen-bonding/electrostatic interactions with CoA are not strictly conserved in the family. The CoA interaction of the single-domain CoA-binding proteins is significantly different and much more extensive than that of the multi-subunit/multi-domain CoA-binding protein succinyl-CoA synthetase.
Authors:
Takuya B Hiyama; Min Zhao; Yu Kitago; Min Yao; Shun-Ichi Sekine; Takaho Terada; Chizu Kuroishi; Zhi-Jie Liu; John P Rose; Seiki Kuramitsu; Mikako Shirouzu; Nobuhisa Watanabe; Shigeyuki Yokoyama; Isao Tanaka; Bi-Cheng Wang
Related Documents :
3745183 - Removal of ferredoxin:nadp+ oxidoreductase from thylakoid membranes, rebinding to deple...
8313 - Affinity chromatography and binding studies on immobilized 5'-monophosphate and adenosi...
17456603 - Human prion proteins with pathogenic mutations share common conformational changes resu...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-03-07
Journal Detail:
Title:  Journal of structural and functional genomics     Volume:  7     ISSN:  1345-711X     ISO Abbreviation:  J. Struct. Funct. Genomics     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2007-07-12     Completed Date:  2007-09-19     Revised Date:  2007-12-03    
Medline Journal Info:
Nlm Unique ID:  101128185     Medline TA:  J Struct Funct Genomics     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  119-29     Citation Subset:  IM    
Affiliation:
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Data Bank Information
Bank Name/Acc. No.:
PDB/1Y81;  2D59;  2D5A;  2E6U
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Carrier Proteins / chemistry,  metabolism*
Coenzyme A / chemistry,  metabolism*
Crystallography, X-Ray
Molecular Sequence Data
Protein Binding / physiology
Protein Structure, Tertiary
Pyrococcus horikoshii / metabolism*
Grant Support
ID/Acronym/Agency:
GM60329/GM/NIGMS NIH HHS; GM62407/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 85-61-0/Coenzyme A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LD...
Next Document:  Quality-of-life outcome after hallux valgus surgery.