1bgs: Difference between revisions

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 ==RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR==
-<StructureSection load='1bgs' size='340' side='right' caption='[[1bgs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='1bgs' size='340' side='right'caption='[[1bgs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bgs]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BGS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bgs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BGS FirstGlance]. <br>
-</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=1bgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgs OCA], [http://pdbe.org/1bgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bgs RCSB], [http://www.ebi.ac.uk/pdbsum/1bgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgs ProSAT]</span></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]] 2.6&#8491;</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=1bgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgs OCA], [https://pdbe.org/1bgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bgs RCSB], [https://www.ebi.ac.uk/pdbsum/1bgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM]] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. [[http://www.uniprot.org/uniprot/BARS_BACAM BARS_BACAM]] Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex.
+[https://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgs_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgs_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ 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=1bgs ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-BACKGROUND: Protein-protein recognition is fundamental to most biological processes. The information we have so far on the interfaces between proteins comes largely from several protease-inhibitor and antigen-antibody complexes. Barnase, a bacterial ribonuclease, and barstar, its natural inhibitor, form a tight complex which provides a good model for the study and design of protein-protein non-covalent interactions. RESULTS: Here we report the structure of a complex between barnase and a fully functional mutant of barstar determined by X-ray analysis. Barstar is composed of three parallel alpha-helices stacked against a three-stranded parallel, beta-sheet, and sterically blocks the active site of the enzyme with an alpha-helix and adjacent loop. The buried surface in the interface between the two molecules totals 1630 A2. The barnase-barstar complex is predominantly stabilized by charge interactions involving positive charges in the active site of the enzyme. Asp39 of barstar binds to the phosphate-binding site of barnase, mimicking enzyme-substrate interactions. CONCLUSION: The phosphate-binding site of the enzyme is the anchor point for inhibitor binding. We propose that this is also likely to be the case for other ribonuclease inhibitors.
-Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar.,Guillet V, Lapthorn A, Hartley RW, Mauguen Y Structure. 1993 Nov 15;1(3):165-76. PMID:16100951<ref>PMID:16100951</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1bgs" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Barnase|Barnase]]
+*[[Barnase 3D structures|Barnase 3D structures]]
-*[[Barstar|Barstar]]
+*[[Barstar 3D structures|Barstar 3D structures]]
-*[[Ribonuclease|Ribonuclease]]
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-*[[Temp|Temp]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Guillet, V]]
+[[Category: Bacillus amyloliquefaciens]]
-[[Category: Lapthorn, A]]
+[[Category: Large Structures]]
-[[Category: Mauguen, Y]]
+[[Category: Guillet V]]
-[[Category: Endonuclease]]
+[[Category: Lapthorn A]]
+[[Category: Mauguen Y]]