1yvs

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[[Image:1yvs.jpg|left|200px]]
 
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{{Structure
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==Trimeric domain swapped barnase==
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|PDB= 1yvs |SIZE=350|CAPTION= <scene name='initialview01'>1yvs</scene>, resolution 2.2&Aring;
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<StructureSection load='1yvs' size='340' side='right'caption='[[1yvs]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1yvs]] is a 1 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=1YVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVS FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1yvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvs OCA], [https://pdbe.org/1yvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yvs RCSB], [https://www.ebi.ac.uk/pdbsum/1yvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvs ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvs OCA], [http://www.ebi.ac.uk/pdbsum/1yvs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yvs RCSB]</span>
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== Function ==
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}}
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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/yv/1yvs_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=1yvs 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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The structure of a trimeric domain-swapped form of barnase (EC 3.1. 27.3) was determined by x-ray crystallography at a resolution of 2.2 A from crystals of space group R32. Residues 1-36 of one molecule associate with residues 41-110 from another molecule related through threefold symmetry. The resulting cyclic trimer contains three protein folds that are very similar to those in monomeric barnase. Both swapped domains contain a nucleation site for folding. The formation of a domain-swapped trimer is consistent with the description of the folding process of monomeric barnase as the formation and subsequent association of two foldons.
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'''TRIMERIC DOMAIN SWAPPED BARNASE'''
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Trimeric domain-swapped barnase.,Zegers I, Deswarte J, Wyns L Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):818-22. PMID:9927651<ref>PMID:9927651</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1yvs" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of a trimeric domain-swapped form of barnase (EC 3.1. 27.3) was determined by x-ray crystallography at a resolution of 2.2 A from crystals of space group R32. Residues 1-36 of one molecule associate with residues 41-110 from another molecule related through threefold symmetry. The resulting cyclic trimer contains three protein folds that are very similar to those in monomeric barnase. Both swapped domains contain a nucleation site for folding. The formation of a domain-swapped trimer is consistent with the description of the folding process of monomeric barnase as the formation and subsequent association of two foldons.
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*[[Barnase 3D structures|Barnase 3D structures]]
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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==About this Structure==
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== References ==
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1YVS is a [[Single protein]] structure of sequence 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=1YVS OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Trimeric domain-swapped barnase., Zegers I, Deswarte J, Wyns L, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):818-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9927651 9927651]
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[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Wyns, L.]]
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[[Category: Wyns L]]
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[[Category: Zegers, I.]]
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[[Category: Zegers I]]
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[[Category: domain swapped]]
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[[Category: endonuclease]]
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[[Category: ribonuclease]]
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[[Category: trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:24:26 2008''
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Current revision

Trimeric domain swapped barnase

PDB ID 1yvs

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