| Structural basis of CoA recognition by the Pyrococcus single-domain CoA-binding proteins. | |
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MedLine Citation:
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PMID: 17342453 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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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 |
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Publication Detail:
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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:
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Title: Journal of structural and functional genomics Volume: 7 ISSN: 1345-711X ISO Abbreviation: J. Struct. Funct. Genomics Publication Date: 2006 Dec |
Date Detail:
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Created Date: 2007-07-12 Completed Date: 2007-09-19 Revised Date: 2007-12-03 |
Medline Journal Info:
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Nlm Unique ID: 101128185 Medline TA: J Struct Funct Genomics Country: Netherlands |
Other Details:
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Languages: eng Pagination: 119-29 Citation Subset: IM |
Affiliation:
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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.:
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PDB/1Y81; 2D59; 2D5A; 2E6U |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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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:
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GM60329/GM/NIGMS NIH HHS; GM62407/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 85-61-0/Coenzyme A |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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