2oy5: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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 1.80&Aring;" />
-'''The crystal structure of OspA mutant'''<br />
-==About this Structure==
+==The crystal structure of OspA mutant==
-OY5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OY5 OCA].
+<StructureSection load='2oy5' size='340' side='right'caption='[[2oy5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-[[Category: Borrelia burgdorferi]]
+== Structural highlights ==
-[[Category: Single protein]]
+<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>
-[[Category: Biancalana, M.]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-[[Category: Koide, S.]]
+<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>
-[[Category: Makabe, K.]]
+</table>
-[[Category: Terechko, V.]]
+== Function ==
-[[Category: Yan, S.]]
+[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU]
-[[Category: beta-sheet]]
+== Evolutionary Conservation ==
-[[Category: membrane protein]]
+[[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.
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar  5 13:21:21 2008''
+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&reg;/PubMed&reg;, 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]]