1bgs: Difference between revisions

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[[Image:1bgs.jpg|left|200px]]


{{Structure
==RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR==
|PDB= 1bgs |SIZE=350|CAPTION= <scene name='initialview01'>1bgs</scene>, resolution 2.6&Aring;
<StructureSection load='1bgs' size='340' side='right'caption='[[1bgs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1bgs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bgs RCSB]</span>
[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>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR'''
==See Also==
 
*[[Barnase 3D structures|Barnase 3D structures]]
 
*[[Barstar 3D structures|Barstar 3D structures]]
==Overview==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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.
__TOC__
 
</StructureSection>
==About this Structure==
1BGS is a [[Protein complex]] structure of sequences from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/16100951 16100951]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Guillet, V.]]
[[Category: Guillet V]]
[[Category: Lapthorn, A.]]
[[Category: Lapthorn A]]
[[Category: Mauguen, Y.]]
[[Category: Mauguen Y]]
[[Category: endonuclease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:39 2008''

Latest revision as of 06:36, 7 February 2024

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

1bgs, resolution 2.60Å

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