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2pi3
From Proteopedia
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==The crystal structure of OspA mutant== | ==The crystal structure of OspA mutant== | ||
| - | <StructureSection load='2pi3' size='340' side='right' caption='[[2pi3]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='2pi3' size='340' side='right'caption='[[2pi3]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2pi3]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2pi3]] 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=2PI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PI3 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</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=2pi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pi3 OCA], [https://pdbe.org/2pi3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pi3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pi3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pi3 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q45040_BORBG Q45040_BORBG] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pi3_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pi3_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=2pi3 ConSurf]. |
<div style="clear:both"></div> | <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 2pi3" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Outer surface protein|Outer surface protein]] | *[[Outer surface protein|Outer surface protein]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Borreliella burgdorferi]] |
| - | [[Category: Biancalana | + | [[Category: Large Structures]] |
| - | [[Category: Koide | + | [[Category: Biancalana M]] |
| - | [[Category: Makabe | + | [[Category: Koide S]] |
| - | [[Category: Terechko | + | [[Category: Makabe K]] |
| - | + | [[Category: Terechko V]] | |
| - | + | ||
Current revision
The crystal structure of OspA mutant
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