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| | <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 [https://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. 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> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ol6|2ol6]], [[2ol7|2ol7]], [[2ol8|2ol8]], [[2oy1|2oy1]], [[2oy5|2oy5]], [[2oy7|2oy7]], [[2oy8|2oy8]], [[2oyb|2oyb]]</div></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]] 1.4Å</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>
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| | <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'>[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> |
| | </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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35210]] | + | [[Category: Borreliella burgdorferi]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Biancalana, M]] | + | [[Category: Biancalana M]] |
| - | [[Category: Koide, S]] | + | [[Category: Koide S]] |
| - | [[Category: Makabe, K]] | + | [[Category: Makabe K]] |
| - | [[Category: Terechko, V]] | + | [[Category: Terechko V]] |
| - | [[Category: Beta sheet]]
| + | |
| - | [[Category: Membrane protein]]
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| Structural highlights
Function
Q45040_BORBG
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
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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