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| <StructureSection load='2i5z' size='340' side='right'caption='[[2i5z]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='2i5z' size='340' side='right'caption='[[2i5z]], [[Resolution|resolution]] 1.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2i5z]] 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=2I5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I5Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2i5z]] 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=2I5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I5Z FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=2i5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i5z OCA], [https://pdbe.org/2i5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i5z RCSB], [https://www.ebi.ac.uk/pdbsum/2i5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i5z 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=2i5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i5z OCA], [https://pdbe.org/2i5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i5z RCSB], [https://www.ebi.ac.uk/pdbsum/2i5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i5z ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Atcc 35210]] | + | [[Category: Borreliella burgdorferi]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Koide, S]] | + | [[Category: Koide S]] |
- | [[Category: Makabe, K]] | + | [[Category: Makabe K]] |
- | [[Category: Terechko, V]] | + | [[Category: Terechko V]] |
- | [[Category: Beta-sheet]]
| + | |
- | [[Category: De novo protein]]
| + | |
| Structural highlights
Function
OSPA_BORBU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Formation of a flat beta-sheet is a fundamental event in beta-sheet-mediated protein self-assembly. To investigate the contributions of various factors to the stability of flat beta-sheets, we performed extensive alanine-scanning mutagenesis experiments on the single-layer beta-sheet segment of Borrelia outer surface protein A (OspA). This beta-sheet segment consists of beta-strands with highly regular geometries that can serve as a building block for self-assembly. Our Ala-scanning approach is distinct from the conventional host-guest method, in that it introduces only conservative, truncation mutations that should minimize structural perturbation. Our results showed very weak correlation with experimental beta-sheet propensity scales, statistical beta-sheet propensity scales, or cross-strand pairwise correlations. In contrast, our data showed strong positive correlation with the change in buried non-polar surface area. Polar interactions including prominent Glu-Lys cross-strand pairs contribute marginally to the beta-sheet stability. These results were corroborated by results from additional non-Ala mutations. Taken together, these results demonstrate the dominant contribution of non-polar surface burial to flat beta-sheet stability even at solvent-exposed positions. The OspA single-layer beta-sheet achieves efficient hydrophobic surface burial without forming a hydrophobic core by a strategic placement of a variety of side-chains. These findings further suggest the importance of hydrophobic interactions within a beta-sheet layer in peptide self-assembly.
Hydrophobic surface burial is the major stability determinant of a flat, single-layer beta-sheet.,Yan S, Gawlak G, Makabe K, Tereshko V, Koide A, Koide S J Mol Biol. 2007 Apr 20;368(1):230-43. Epub 2007 Feb 7. PMID:17335845[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yan S, Gawlak G, Makabe K, Tereshko V, Koide A, Koide S. Hydrophobic surface burial is the major stability determinant of a flat, single-layer beta-sheet. J Mol Biol. 2007 Apr 20;368(1):230-43. Epub 2007 Feb 7. PMID:17335845 doi:10.1016/j.jmb.2007.02.003
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