6g8d - Revision history

OCA at 07:33, 1 May 2024

OCA — Wed, 01 May 2024 07:33:48 GMT

←Older revision		Revision as of 07:33, 1 May 2024
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	<StructureSection load='6g8d' size='340' side='right'caption='[[6g8d]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='6g8d' size='340' side='right'caption='[[6g8d]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6g8d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G8D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6G8D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6g8d]] is a 1 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=6G8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G8D 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=6g8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g8d OCA], [~~http~~://pdbe.org/6g8d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6g8d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6g8d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6g8d 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]] 1.85Å</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=6g8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g8d OCA], [https://pdbe.org/6g8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g8d RCSB], [https://www.ebi.ac.uk/pdbsum/6g8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g8d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[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.	+	[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.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	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.	+
-		+
-	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>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6g8d" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Landau, M]]	+	[[Category: Landau M]]
-	[[Category: Perov, S]]	+	[[Category: Perov S]]
-	~~[[Category: Bacterial steric-zipper cross-beta amyloid fibril from e. coli]]~~	+
-	~~[[Category: Protein fibril~~]]	+

OCA at 07:53, 23 October 2019

OCA — Wed, 23 Oct 2019 07:53:01 GMT

←Older revision		Revision as of 07:53, 23 October 2019
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	== Function ==		== Function ==
	[[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.		[[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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.
		+
		+	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>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6g8d" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:41, 24 April 2019

OCA — Wed, 24 Apr 2019 06:41:20 GMT

←Older revision		Revision as of 06:41, 24 April 2019
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-	'''Unreleased structure'''

-	~~The entry 6g8d is ON HOLD until Paper Publication~~	+	==Crystal Structure of the Amyloid-like LNIYQY segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein==
-		+	<StructureSection load='6g8d' size='340' side='right'caption='[[6g8d]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~Authors: Landau, M., Perov, S.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6g8d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G8D FirstGlance]. <br>
-	~~Description:~~ Crystal Structure of the Amyloid-like LNIYQY segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein	+	</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=6g8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g8d OCA], [http://pdbe.org/6g8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g8d RCSB], [http://www.ebi.ac.uk/pdbsum/6g8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g8d ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	== Function ==
		+	[[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.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Landau, M]]
	[[Category: Perov, S]]		[[Category: Perov, S]]
-	[[Category: ~~Landau, M~~]]	+	[[Category: Bacterial steric-zipper cross-beta amyloid fibril from e. coli]]
		+	[[Category: Protein fibril]]

OCA at 04:17, 25 April 2018

OCA — Wed, 25 Apr 2018 04:17:14 GMT

←Older revision		Revision as of 04:17, 25 April 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6g8d is ON HOLD	+	The entry 6g8d is ON HOLD until Paper Publication

	Authors: Landau, M., Perov, S.		Authors: Landau, M., Perov, S.

-	Description: Crystal Structure of the Amyloid-like ~~IYQYGG~~ segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein	+	Description: Crystal Structure of the Amyloid-like LNIYQY segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Perov, S]]		[[Category: Perov, S]]
	[[Category: Landau, M]]		[[Category: Landau, M]]

OCA: Protected "6g8d" [edit=sysop:move=sysop]

OCA — Wed, 18 Apr 2018 04:27:52 GMT

Protected "6g8d" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:27, 18 April 2018

OCA: New page: '''Unreleased structure''' The entry 6g8d is ON HOLD Authors: Landau, M., Perov, S. Description: Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli ...

OCA — Wed, 18 Apr 2018 04:27:51 GMT

New page: '''Unreleased structure''' The entry 6g8d is ON HOLD Authors: Landau, M., Perov, S. Description: Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli ...

New page

'''Unreleased structure'''

The entry 6g8d is ON HOLD

Authors: Landau, M., Perov, S.

Description: Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
[[Category: Unreleased Structures]]
[[Category: Perov, S]]
[[Category: Landau, M]]