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6g8e

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Current revision (07:33, 1 May 2024) (edit) (undo)
 
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<StructureSection load='6g8e' size='340' side='right'caption='[[6g8e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6g8e' size='340' side='right'caption='[[6g8e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6g8e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G8E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6g8e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G8E FirstGlance]. <br>
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</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=6g8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g8e OCA], [http://pdbe.org/6g8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g8e RCSB], [http://www.ebi.ac.uk/pdbsum/6g8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g8e ProSAT]</span></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]] 1.7&#8491;</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=6g8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g8e OCA], [https://pdbe.org/6g8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g8e RCSB], [https://www.ebi.ac.uk/pdbsum/6g8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g8e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CSGA_ECOLI CSGA_ECOLI]] Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin.
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[https://www.uniprot.org/uniprot/CSGA_ECOLI CSGA_ECOLI] Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming segments from the major curli subunit, CsgA, revealing steric zipper fibrils of tightly mated beta-sheets, demonstrating a structural link between curli and human pathological amyloids. D-enantiomeric peptides, originally developed to interfere with Alzheimer's disease-associated amyloid-beta, inhibited CsgA fibrillation and reduced biofilm formation in Salmonella typhimurium. Moreover, as previously shown, CsgA fibrils cross-seeded fibrillation of amyloid-beta, providing support for the proposed structural resemblance and potential for cross-species amyloid interactions. The presented findings provide structural insights into amyloidogenic regions important for curli formation, suggest a novel strategy for disrupting amyloid-structured biofilms, and hypothesize on the formation of self-propagating prion-like species originating from a microbial source that could influence neurodegenerative diseases.
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Structural Insights into Curli CsgA Cross-beta Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.,Perov S, Lidor O, Salinas N, Golan N, Tayeb-Fligelman E, Deshmukh M, Willbold D, Landau M PLoS Pathog. 2019 Aug 30;15(8):e1007978. doi: 10.1371/journal.ppat.1007978., eCollection 2019 Aug. PMID:31469892<ref>PMID:31469892</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 6g8e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Landau, M]]
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[[Category: Landau M]]
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[[Category: Perov, S]]
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[[Category: Perov S]]
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[[Category: Bacterial steric-zipper cross-beta amyloid fibril from e. coli]]
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[[Category: Protein fibril]]
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Current revision

Crystal Structure of the Amyloid-like VTQVGF segment from the R5 repeat of the E. coli Biofilm-associated CsgA Curli protein

PDB ID 6g8e

Drag the structure with the mouse to rotate

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