6fg4
From Proteopedia
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<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=6fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fg4 OCA], [http://pdbe.org/6fg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fg4 RCSB], [http://www.ebi.ac.uk/pdbsum/6fg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fg4 ProSAT]</span></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=6fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fg4 OCA], [http://pdbe.org/6fg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fg4 RCSB], [http://www.ebi.ac.uk/pdbsum/6fg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fg4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Members of the Staphylococcus aureus phenol-soluble modulin (PSM) peptide family are secreted as functional amyloids that serve diverse roles in pathogenicity and may be present as full-length peptides or as naturally occurring truncations. We recently showed that the activity of PSMalpha3, the most toxic member, stems from the formation of cross-alpha fibrils, which are at variance with the cross-beta fibrils linked with eukaryotic amyloid pathologies. Here, we show that PSMalpha1 and PSMalpha4, involved in biofilm structuring, form canonical cross-beta amyloid fibrils wherein beta-sheets tightly mate through steric zipper interfaces, conferring high stability. Contrastingly, a truncated PSMalpha3 has antibacterial activity, forms reversible fibrils, and reveals two polymorphic and atypical beta-rich fibril architectures. These architectures are radically different from both the cross-alpha fibrils formed by full-length PSMalpha3, and from the canonical cross-beta fibrils. Our results point to structural plasticity being at the basis of the functional diversity exhibited by S. aureus PSMalphas. | ||
| + | |||
| + | Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMalpha peptides.,Salinas N, Colletier JP, Moshe A, Landau M Nat Commun. 2018 Aug 29;9(1):3512. doi: 10.1038/s41467-018-05490-0. PMID:30158633<ref>PMID:30158633</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6fg4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:53, 12 September 2018
Crystal Structure of the Amyloid-like IIKVIK Segment from the S. aureus Biofilm-associated PSMalpha1
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