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| | <StructureSection load='2oyb' size='340' side='right'caption='[[2oyb]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='2oyb' size='340' side='right'caption='[[2oyb]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oyb]] 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=2OYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OYB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oyb]] 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=2OYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OYB 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;'>[[2oy1|2oy1]], [[2oy5|2oy5]], [[2oy7|2oy7]], [[2oy8|2oy8]]</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]] 1.3Å</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=2oyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyb OCA], [https://pdbe.org/2oyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oyb RCSB], [https://www.ebi.ac.uk/pdbsum/2oyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oyb 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=2oyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyb OCA], [https://pdbe.org/2oyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oyb RCSB], [https://www.ebi.ac.uk/pdbsum/2oyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oyb 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: 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]]
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| - | [[Category: Membrane protein]]
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| 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
Though beta-rich self-assemblies comprise a major structural class of polypeptides, a detailed understanding of the determinants of their structure and stability is lacking. In particular, the roles of repetitive stretches of side chains running the long axis of these beta-sheets, termed "cross-strand ladders," remain poorly characterized due to the inherently insoluble and heterogeneous nature of self-assemblies. To overcome these experimental challenges, we have established a complementary experimental system termed "peptide self-assembly mimics" (PSAMs). The PSAMs capture a defined number of self-assembly-like peptide repeats within a soluble beta-rich protein, making structural and energetic studies possible. In this work, we investigated the role of cross-strand ladders containing aromatic residues, which are prominent in self-assembling peptides. A combination of solution data and high-resolution crystal structures revealed that a single cross-strand ladder consisting solely of Tyr significantly stabilized, rigidified, and flattened the PSAM beta-sheet. These characteristics would stabilize each beta-sheet layer of a self-assembly and direct sheet conformations compatible with lamination. Our results therefore provide a rationale for the abundance of aromatic amino acids in fibril-forming peptides and establish important roles of cross-strand Tyr ladders in the structure and stability of beta-rich peptide self-assemblies.
Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics.,Biancalana M, Makabe K, Koide A, Koide S J Mol Biol. 2008 Oct 31;383(1):205-13. Epub 2008 Aug 22. PMID:18762191[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Biancalana M, Makabe K, Koide A, Koide S. Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics. J Mol Biol. 2008 Oct 31;383(1):205-13. Epub 2008 Aug 22. PMID:18762191 doi:10.1016/j.jmb.2008.08.031
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