1b2s

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{{Seed}}
 
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[[Image:1b2s.png|left|200px]]
 
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==STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE==
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The line below this paragraph, containing "STRUCTURE_1b2s", creates the "Structure Box" on the page.
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<StructureSection load='1b2s' size='340' side='right'caption='[[1b2s]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1b2s]] 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=1B2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B2S FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.82&#8491;</td></tr>
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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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{{STRUCTURE_1b2s| PDB=1b2s | SCENE= }}
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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=1b2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b2s OCA], [https://pdbe.org/1b2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b2s RCSB], [https://www.ebi.ac.uk/pdbsum/1b2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b2s 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/b2/1b2s_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=1b2s 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 have crystallised three mutants of the barnase-barstar complex in which interactions across the interface have been deleted by simultaneous mutation of both residues involved in the interaction. Each mutant deletes a different type of interaction at the interface: the first complex bnHis102--&gt;Ala-bsTyr29--&gt;Phe (bn, barnase; bs, barstar), deletes a van der Waals packing interaction; the second complex, bnLys27--&gt;Ala-bsThr42--&gt;Ala, deletes a hydrogen bond; the third, bnLys27--&gt;Ala-bsAsp35--&gt;Ala, deletes a long-range charge-charge interaction. The contribution of each of these side-chains to the stability of the complex is known; the coupling energy between the deleted side-chains is also known. Despite each of the double mutants being significantly destabilised compared with the wild-type, the effects of mutation are local. Only small movements in the main-chain surrounding the sites of mutation and some larger movements of neighbouring side-chains are observed in the mutant complexes. The exact response to mutation is context-dependent and for the same mutant can vary depending upon the environment within the crystal. In some double mutant complexes, interfacial pockets, which are accessible to bulk solvent are formed, whereas interfacial cavities which are isolated from bulk solvent, are formed in others. In all double mutants, water molecules fill the created pockets and cavities. These water molecules mimic the deleted side-chains by occupying positions close to the non-carbon atoms of truncated side-chains and re-making many hydrogen bonds made by the truncated side-chains in the wild-type. It remains extremely difficult, however, to correlate energetic and structural responses to mutation because of unknown changes in entropy and entropy-enthalpy compensation.
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===STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE===
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Structural response to mutation at a protein-protein interface.,Vaughan CK, Buckle AM, Fersht AR J Mol Biol. 1999 Mar 12;286(5):1487-506. PMID:10064711<ref>PMID:10064711</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 1b2s" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10064711}}, adds the Publication Abstract to the page
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*[[Barnase 3D structures|Barnase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10064711 is the PubMed ID number.
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*[[Barstar 3D structures|Barstar 3D structures]]
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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{{ABSTRACT_PUBMED_10064711}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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1B2S 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=1B2S OCA].
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</StructureSection>
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==Reference==
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Structural response to mutation at a protein-protein interface., Vaughan CK, Buckle AM, Fersht AR, J Mol Biol. 1999 Mar 12;286(5):1487-506. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10064711 10064711]
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[[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: Buckle, A M.]]
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[[Category: Buckle AM]]
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[[Category: Fersht, A R.]]
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[[Category: Fersht AR]]
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[[Category: Vaughan, C K.]]
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[[Category: Vaughan CK]]
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[[Category: Interfacial double mutant]]
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[[Category: Rnase-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:05:58 2008''
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Current revision

STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE

PDB ID 1b2s

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