2d59: Difference between revisions

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OCA

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 ==hypothetical protein from Pyrococcus horikoshii OT3==
-<StructureSection load='2d59' size='340' side='right' caption='[[2d59]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+<StructureSection load='2d59' size='340' side='right'caption='[[2d59]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d59]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D59 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d59]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D59 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d5a|2d5a]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ph1109 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d59 OCA], [https://pdbe.org/2d59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d59 RCSB], [https://www.ebi.ac.uk/pdbsum/2d59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d59 ProSAT], [https://www.topsan.org/Proteins/RSGI/2d59 TOPSAN]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d59 OCA], [http://pdbe.org/2d59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d59 RCSB], [http://www.ebi.ac.uk/pdbsum/2d59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d59 ProSAT], [http://www.topsan.org/Proteins/RSGI/2d59 TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O58836_PYRHO O58836_PYRHO]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2d59 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-Structural basis of CoA recognition by the Pyrococcus single-domain CoA-binding proteins.,Hiyama TB, Zhao M, Kitago Y, Yao M, Sekine S, Terada T, Kuroishi C, Liu ZJ, Rose JP, Kuramitsu S, Shirouzu M, Watanabe N, Yokoyama S, Tanaka I, Wang BC J Struct Funct Genomics. 2006 Dec;7(3-4):119-29. Epub 2007 Mar 7. PMID:17342453<ref>PMID:17342453</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2d59" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Pyrococcus horikoshii]]
+[[Category: Large Structures]]
-[[Category: Hiyama, T B]]
+[[Category: Pyrococcus horikoshii OT3]]
-[[Category: Structural genomic]]
+[[Category: Hiyama TB]]
-[[Category: Sekine, S]]
+[[Category: Sekine S]]
-[[Category: Yokoyama, S]]
+[[Category: Yokoyama S]]
-[[Category: Coa binding]]
-[[Category: Hypothetical protein]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Rsgi]]
-[[Category: Unknown function]]