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| | <StructureSection load='2af5' size='340' side='right'caption='[[2af5]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2af5' size='340' side='right'caption='[[2af5]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2af5]] 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=2AF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AF5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2af5]] 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=2AF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AF5 FirstGlance]. <br> |
| - | </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=2af5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2af5 OCA], [http://pdbe.org/2af5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2af5 RCSB], [http://www.ebi.ac.uk/pdbsum/2af5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2af5 ProSAT]</span></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]] 2.5Å</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=2af5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2af5 OCA], [https://pdbe.org/2af5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2af5 RCSB], [https://www.ebi.ac.uk/pdbsum/2af5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2af5 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: Hilyard, A]] | + | [[Category: Hilyard A]] |
| - | [[Category: Koide, A]] | + | [[Category: Koide A]] |
| - | [[Category: Koide, S]] | + | [[Category: Koide S]] |
| - | [[Category: Makabe, K]] | + | [[Category: Makabe K]] |
| - | [[Category: Mcelheny, D]] | + | [[Category: Mcelheny D]] |
| - | [[Category: Tereshko, V]] | + | [[Category: Tereshko V]] |
| - | [[Category: Beta-hairpin]]
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| - | [[Category: De novo protein]]
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| - | [[Category: Immune system]]
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| - | [[Category: Repeat protein]]
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| - | [[Category: Single-layer beta-sheet]]
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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
Although the beta-rich self-assemblies are a major structural class for polypeptides and the focus of intense research, little is known about their atomic structures and dynamics due to their insoluble and noncrystalline nature. We developed a protein engineering strategy that captures a self-assembly segment in a water-soluble molecule. A predefined number of self-assembling peptide units are linked, and the beta-sheet ends are capped to prevent aggregation, which yields a mono-dispersed soluble protein. We tested this strategy by using Borrelia outer surface protein (OspA) whose single-layer beta-sheet located between two globular domains consists of two beta-hairpin units and thus can be considered as a prototype of self-assembly. We constructed self-assembly mimics of different sizes and determined their atomic structures using x-ray crystallography and NMR spectroscopy. Highly regular beta-sheet geometries were maintained in these structures, and peptide units had a nearly identical conformation, supporting the concept that a peptide in the regular beta-geometry is primed for self-assembly. However, we found small but significant differences in the relative orientation between adjacent peptide units in terms of beta-sheet twist and bend, suggesting their inherent flexibility. Modeling shows how this conformational diversity, when propagated over a large number of peptide units, can lead to a substantial degree of nanoscale polymorphism of self-assemblies.
Atomic structures of peptide self-assembly mimics.,Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:17093048[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S. Atomic structures of peptide self-assembly mimics. Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:17093048
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