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2oy5
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2oy5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oy5, resolution 1.80Å" /> '''The crystal structur...) |
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| - | [[Image:2oy5.jpg|left|200px]]<br /><applet load="2oy5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2oy5, resolution 1.80Å" /> | ||
| - | '''The crystal structure of OspA mutant'''<br /> | ||
| - | == | + | ==The crystal structure of OspA mutant== |
| - | + | <StructureSection load='2oy5' size='340' side='right'caption='[[2oy5]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2oy5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OY5 FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | [ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oy5 OCA], [https://pdbe.org/2oy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oy5 RCSB], [https://www.ebi.ac.uk/pdbsum/2oy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oy5 ProSAT]</span></td></tr> |
| - | [ | + | </table> |
| - | [[ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU] |
| - | [[ | + | == 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/oy/2oy5_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=2oy5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Site-directed mutagenesis is a powerful tool for altering the structure and function of proteins in a focused manner. Here, we examined how a model beta-sheet protein could be tuned by mutation of numerous surface-exposed residues to aromatic amino acids. We designed these aromatic side chain "clusters" at highly solvent-exposed positions in the flat, single-layer beta-sheet of Borrelia outer surface protein A (OspA). This unusual beta-sheet scaffold allows us to interrogate the effects of these mutations in the context of well-defined structure but in the absence of the strong scaffolding effects of globular protein architecture. We anticipated that the introduction of a cluster of aromatic amino acid residues on the beta-sheet surface would result in large conformational changes and/or stabilization and thereby provide new means of controlling the properties of beta-sheets. Surprisingly, X-ray crystal structures revealed that the introduction of aromatic clusters produced only subtle conformational changes in the OspA beta-sheet. Additionally, despite burying a large degree of hydrophobic surface area, the aromatic cluster mutants were slightly less stable than the wild-type scaffold. These results thereby demonstrate that the introduction of aromatic cluster mutations can serve as a means for subtly modulating beta-sheet conformation in protein design. | ||
| - | + | Aromatic cluster mutations produce focal modulations of beta-sheet structure.,Biancalana M, Makabe K, Yan S, Koide S Protein Sci. 2015 May;24(5):841-9. doi: 10.1002/pro.2657. Epub 2015 Mar 25. PMID:25645104<ref>PMID:25645104</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2oy5" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Outer surface protein|Outer surface protein]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Borreliella burgdorferi]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Biancalana M]] | ||
| + | [[Category: Koide S]] | ||
| + | [[Category: Makabe K]] | ||
| + | [[Category: Terechko V]] | ||
| + | [[Category: Yan S]] | ||
Current revision
The crystal structure of OspA mutant
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