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| | ==Crystal structure of OspA mutant== | | ==Crystal structure of OspA mutant== |
| - | <StructureSection load='3aum' size='340' side='right' caption='[[3aum]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3aum' size='340' side='right'caption='[[3aum]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3aum]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AUM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3aum]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 ATCC 35210])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ospA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 ATCC 35210])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aum OCA], [http://pdbe.org/3aum PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aum RCSB], [http://www.ebi.ac.uk/pdbsum/3aum PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aum ProSAT]</span></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> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 35210]] | | [[Category: Atcc 35210]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Makabe, K]] | | [[Category: Makabe, K]] |
| | [[Category: Beta-mender]] | | [[Category: Beta-mender]] |
| | [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Biancalana M, Makabe K, Yan S, Koide S. Aromatic cluster mutations produce focal modulations of beta-sheet structure. Protein Sci. 2015 May;24(5):841-9. doi: 10.1002/pro.2657. Epub 2015 Mar 25. PMID:25645104 doi:http://dx.doi.org/10.1002/pro.2657
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