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| | <StructureSection load='6j49' size='340' side='right'caption='[[6j49]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='6j49' size='340' side='right'caption='[[6j49]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j49]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Borbu Borbu]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5b10 5b10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J49 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5b10 5b10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J49 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ospA, BB_A15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224326 BORBU])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6j49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j49 OCA], [http://pdbe.org/6j49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j49 RCSB], [http://www.ebi.ac.uk/pdbsum/6j49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j49 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=6j49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j49 OCA], [https://pdbe.org/6j49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j49 RCSB], [https://www.ebi.ac.uk/pdbsum/6j49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j49 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Borbu]] | + | [[Category: Borreliella burgdorferi B31]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hori, Y]] | + | [[Category: Hori Y]] |
| - | [[Category: Makabe, K]] | + | [[Category: Makabe K]] |
| - | [[Category: Beta-sheet]]
| + | |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| Structural highlights
Function
OSPA_BORBU
Publication Abstract from PubMed
Many protein and peptide sequences are self-assembled into beta-sheet-rich fibrous structures called amyloids. Their atomic details provide insights into fundamental knowledge related to amyloid diseases. To study the detailed structure of the amyloid, we have developed a model system that mimics the self-assembling process of the amyloid within a water-soluble protein, termed peptide self-assembly mimic (PSAM). PSAM enables capturing of a peptide sequence within a water-soluble protein, thus making structural and energetics-related studies possible. In this work, we extend our PSAM approach to a naturally occurring chameleon sequence from alphaB crystallin. We chose "Val-Leu-Gly-Asp-Val (VLGDV)", a five amino-acid sequence, which forms a beta-turn in the native structure and a beta-barrel in the amyloid oligomer cylindrin, as a grafting sequence to the PSAM scaffold. The crystal structure revealed that the sequence grafting induced beta-sheet bending at the grafted site. We further investigated the role of the central glycine residue and found that its role in the beta-sheet bending is dependent on the neighboring residues. The ability of PSAM to observe the structural alterations induced by the grafted sequence provides an opportunity to evaluate the structural impact of a sequence from the peptide self-assembly.
Grafting a short chameleon sequence from alphaB crystallin into a beta-sheet scaffold protein.,Hori Y, Fujiwara H, Fujiwara W, Makabe K Proteins. 2019 Jan 26. doi: 10.1002/prot.25663. PMID:30684364[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hori Y, Fujiwara H, Fujiwara W, Makabe K. Grafting a short chameleon sequence from alphaB crystallin into a beta-sheet scaffold protein. Proteins. 2019 Jan 26. doi: 10.1002/prot.25663. PMID:30684364 doi:http://dx.doi.org/10.1002/prot.25663
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