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1bgs

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(New page: 200px<br /><applet load="1bgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bgs, resolution 2.6&Aring;" /> '''RECOGNITION BETWEEN A...)
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[[Image:1bgs.jpg|left|200px]]<br /><applet load="1bgs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bgs, resolution 2.6&Aring;" />
 
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'''RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR'''<br />
 
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==Overview==
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==RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR==
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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.
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<StructureSection load='1bgs' size='340' side='right'caption='[[1bgs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BGS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BGS OCA].
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*[[Barnase 3D structures|Barnase 3D structures]]
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*[[Barstar 3D structures|Barstar 3D structures]]
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==Reference==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16100951 16100951]
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__TOC__
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</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Guillet, V.]]
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[[Category: Guillet V]]
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[[Category: Lapthorn, A.]]
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[[Category: Lapthorn A]]
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[[Category: Mauguen, Y.]]
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[[Category: Mauguen Y]]
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[[Category: endonuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:38:39 2007''
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Current revision

RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR

PDB ID 1bgs

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