View source for 3aum


==Crystal structure of OspA mutant==
<StructureSection load='3aum' size='340' side='right'caption='[[3aum]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3aum]] 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=3AUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AUM 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]] 1.6&#8491;</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=3aum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aum OCA], [https://pdbe.org/3aum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aum RCSB], [https://www.ebi.ac.uk/pdbsum/3aum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aum ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3aum" style="background-color:#fffaf0;"></div>

==See Also==
*[[Outer surface protein|Outer surface protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borreliella burgdorferi]]
[[Category: Large Structures]]
[[Category: Makabe K]]