6fgr

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Current revision (07:32, 1 May 2024) (edit) (undo)
 
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<StructureSection load='6fgr' size='340' side='right'caption='[[6fgr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6fgr' size='340' side='right'caption='[[6fgr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6fgr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FGR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6fgr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FGR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6fg4|6fg4]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6fgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fgr OCA], [https://pdbe.org/6fgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fgr RCSB], [https://www.ebi.ac.uk/pdbsum/6fgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fgr 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=6fgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fgr OCA], [https://pdbe.org/6fgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fgr RCSB], [https://www.ebi.ac.uk/pdbsum/6fgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fgr ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/H9BRQ8_STAAU H9BRQ8_STAAU]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6fgr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Colletier, J P]]
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[[Category: Staphylococcus aureus]]
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[[Category: Landau, M]]
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[[Category: Colletier J-P]]
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[[Category: Bacterial amyloid fibril]]
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[[Category: Landau M]]
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[[Category: Cross-beta]]
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[[Category: Protein fibril]]
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[[Category: Psm]]
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[[Category: S. aureus]]
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[[Category: Steric-zipper]]
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Current revision

Crystal Structure of the Amyloid-like IIKIIK Segment from the S. aureus Biofilm-associated PSMalpha4

PDB ID 6fgr

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OCA

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