1ay7

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(New page: 200px<br /><applet load="1ay7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ay7, resolution 1.7&Aring;" /> '''RIBONUCLEASE SA COMPL...)
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[[Image:1ay7.gif|left|200px]]<br /><applet load="1ay7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ay7, resolution 1.7&Aring;" />
 
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'''RIBONUCLEASE SA COMPLEX WITH BARSTAR'''<br />
 
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==Overview==
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==RIBONUCLEASE SA COMPLEX WITH BARSTAR==
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We report the 1.7 A resolution structure of RNase Sa complexed with the, polypeptide inhibitor barstar. The crystals are in the hexagonal space, group P65 with unit-cell dimensions a = b = 56.9, c = 135.8 A and the, asymmetric unit contains one molecule of the complex. RNase Sa is an, extracellular microbial ribonuclease produced by Streptomyces, aureofaciens. Barstar is the natural inhibitor of barnase, the, ribonuclease of Bacillus amyloliquefaciens. It inhibits RNase Sa and, barnase in a similar manner by steric blocking of the active site. The, structure of RNase Sa is very similar to that observed in crystals of the, native enzyme and its complexes with nucleotides. Barstar retains the, structure found in its complex with barnase. The accessible surface area, of protein buried in the complex is about 300 A2 smaller and there are, fewer hydrogen bonds in the enzyme-inhibitor interface in RNase Sa-barstar, than in barnase-barstar, providing an explanation of the reduced binding, affinity in the former. Previous studies of barstar complexes have used, mutants of the inhibitor and this is the first structure which includes, wild-type barstar.
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<StructureSection load='1ay7' size='340' side='right'caption='[[1ay7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ay7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] and [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AY7 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]] 1.7&#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=1ay7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ay7 OCA], [https://pdbe.org/1ay7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ay7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ay7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ay7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
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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/ay/1ay7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ay7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We report the 1.7 A resolution structure of RNase Sa complexed with the polypeptide inhibitor barstar. The crystals are in the hexagonal space group P65 with unit-cell dimensions a = b = 56.9, c = 135.8 A and the asymmetric unit contains one molecule of the complex. RNase Sa is an extracellular microbial ribonuclease produced by Streptomyces aureofaciens. Barstar is the natural inhibitor of barnase, the ribonuclease of Bacillus amyloliquefaciens. It inhibits RNase Sa and barnase in a similar manner by steric blocking of the active site. The structure of RNase Sa is very similar to that observed in crystals of the native enzyme and its complexes with nucleotides. Barstar retains the structure found in its complex with barnase. The accessible surface area of protein buried in the complex is about 300 A2 smaller and there are fewer hydrogen bonds in the enzyme-inhibitor interface in RNase Sa-barstar than in barnase-barstar, providing an explanation of the reduced binding affinity in the former. Previous studies of barstar complexes have used mutants of the inhibitor and this is the first structure which includes wild-type barstar.
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==About this Structure==
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Recognition of RNase Sa by the inhibitor barstar: structure of the complex at 1.7 A resolution.,Sevcik J, Urbanikova L, Dauter Z, Wilson KS Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):954-63. PMID:9757110<ref>PMID:9757110</ref>
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1AY7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] and [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AY7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Recognition of RNase Sa by the inhibitor barstar: structure of the complex at 1.7 A resolution., Sevcik J, Urbanikova L, Dauter Z, Wilson KS, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):954-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9757110 9757110]
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</div>
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[[Category: Bacillus amyloliquefaciens]]
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<div class="pdbe-citations 1ay7" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Ribonuclease T(1)]]
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[[Category: Streptomyces aureofaciens]]
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[[Category: Dauter, Z.]]
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[[Category: Sevcik, J.]]
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[[Category: Urbanikova, L.]]
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[[Category: Wilson, K.S.]]
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[[Category: complex (enzyme/inhibitor)]]
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[[Category: inhibitor]]
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[[Category: ribonuclease]]
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[[Category: streptomyces aureofaciens]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:11:53 2007''
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==See Also==
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*[[Barstar 3D structures|Barstar 3D structures]]
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus amyloliquefaciens]]
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[[Category: Kitasatospora aureofaciens]]
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[[Category: Large Structures]]
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[[Category: Dauter Z]]
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[[Category: Sevcik J]]
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[[Category: Urbanikova L]]
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[[Category: Wilson KS]]

Current revision

RIBONUCLEASE SA COMPLEX WITH BARSTAR

PDB ID 1ay7

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