4lov - Revision history

OCA at 11:16, 14 December 2022

2022-12-14T11:16:37Z

←Older revision		Revision as of 11:16, 14 December 2022
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	==Crystal structure of FimH in complex with Heptylmannoside==		==Crystal structure of FimH in complex with Heptylmannoside==
-	<StructureSection load='4lov' size='340' side='right' caption='[[4lov]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='4lov' size='340' side='right'caption='[[4lov]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lov]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LOV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LOV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LOV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KGM:HEPTYL+ALPHA-D-MANNOPYRANNOSIDE'>KGM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KGM:HEPTYL+ALPHA-D-MANNOPYRANNOSIDE'>KGM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zpd\|3zpd]]</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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [https://pdbe.org/4lov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [https://www.ebi.ac.uk/pdbsum/4lov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lov ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fimH, b4320, JW4283 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [~~http~~://pdbe.org/4lov PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4lov PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4lov ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.	+	[https://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4lov" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4lov" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Adhesin 3D structures\|Adhesin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
-	[[Category: ~~Garcia-Pino, A~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Nuland, N van~~]]	+	[[Category: Garcia-Pino A]]
-	[[Category: Vanwetswinkel, S]]	+	[[Category: Vanwetswinkel S]]
-	[[Category: ~~Carbohydrate binding protein]]~~	+	[[Category: Van Nuland N]]
-	~~[[Category: Ig fold]]~~	+
-	~~[[Category: Pilus subunit~~]]	+

OCA at 13:38, 5 August 2016

2016-08-05T13:38:53Z

←Older revision		Revision as of 13:38, 5 August 2016
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		+
	==Crystal structure of FimH in complex with Heptylmannoside==		==Crystal structure of FimH in complex with Heptylmannoside==
	<StructureSection load='4lov' size='340' side='right' caption='[[4lov]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='4lov' size='340' side='right' caption='[[4lov]], [[Resolution\|resolution]] 1.50Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zpd\|3zpd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zpd\|3zpd]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fimH, b4320, JW4283 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fimH, b4320, JW4283 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [http://www.ebi.ac.uk/pdbsum/4lov PDBsum]</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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [http://pdbe.org/4lov PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [http://www.ebi.ac.uk/pdbsum/4lov PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lov ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4lov" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:56, 25 December 2014

2014-12-25T02:56:47Z

←Older revision		Revision as of 02:56, 25 December 2014
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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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [http://www.ebi.ac.uk/pdbsum/4lov PDBsum]</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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [http://www.ebi.ac.uk/pdbsum/4lov PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:03, 21 December 2014

2014-12-21T17:03:16Z

←Older revision		Revision as of 17:03, 21 December 2014
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-	~~{{STRUCTURE_4lov\| PDB=4lov \| SCENE= }}~~	+	==Crystal structure of FimH in complex with Heptylmannoside==
-	===Crystal structure of FimH in complex with Heptylmannoside===	+	<StructureSection load='4lov' size='340' side='right' caption='[[4lov]], [[Resolution\|resolution]] 1.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24476493}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4lov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LOV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LOV FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KGM:HEPTYL+ALPHA-D-MANNOPYRANNOSIDE'>KGM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zpd\|3zpd]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fimH, b4320, JW4283 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lov RCSB], [http://www.ebi.ac.uk/pdbsum/4lov PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Uropathogenic Escherichia coli cause urinary tract infections by adhering to mannosylated receptors on the human urothelium via the carbohydrate-binding domain of the FimH adhesin (FimHL). Numerous alpha-d-mannopyranosides, including alpha-d-heptyl mannose (HM), inhibit this process by interacting with FimHL. To establish the molecular basis of the high-affinity HM binding, we solved the solution structure of the apo form and the crystal structure of the FimHL-HM complex. NMR relaxation analysis revealed that protein dynamics were not affected by the sugar binding, yet HM addition promoted protein dimerization, which was further confirmed by small-angle X-ray scattering. Finally, to address the role of Y48, part of the "tyrosine gate" believed to govern the affinity and specificity of mannoside binding, we characterized the FimHL Y48A mutant, whose conformational, dynamical, and HM binding properties were found to be very similar to those of the wild-type protein.

-	~~==Function==~~	+	Study of the Structural and Dynamic Effects in the FimH Adhesin upon alpha-d-Heptyl Mannose Binding.,Vanwetswinkel S, Volkov AN, Sterckx YG, Garcia-Pino A, Buts L, Vranken WF, Bouckaert J, Roy R, Wyns L, van Nuland NA J Med Chem. 2014 Feb 7. PMID:24476493<ref>PMID:24476493</ref>
-	~~[[http://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI]] Involved in regulation~~ of ~~length~~ and ~~mediation of adhesion of type 1 fimbriae (but not necessary for~~ the ~~production of fimbriae).~~ Adhesin ~~responsible for the binding to D~~-~~mannose~~. ~~It is laterally positioned at intervals in the structure of the type 1 fimbriae~~. ~~In order to integrate FimH in the fimbriae FimF and FimG are needed~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4lov]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4LOV OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024476493</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Garcia-Pino, A.]]	+	</StructureSection>
-	[[Category: Nuland, N van.]]	+	[[Category: Bacillus coli migula 1895]]
-	[[Category: Vanwetswinkel, S.]]	+	[[Category: Garcia-Pino, A]]
		+	[[Category: Nuland, N van]]
		+	[[Category: Vanwetswinkel, S]]
	[[Category: Carbohydrate binding protein]]		[[Category: Carbohydrate binding protein]]
	[[Category: Ig fold]]		[[Category: Ig fold]]
	[[Category: Pilus subunit]]		[[Category: Pilus subunit]]

OCA at 05:00, 13 February 2014

2014-02-13T05:00:05Z

←Older revision		Revision as of 05:00, 13 February 2014
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-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4lov\| PDB=4lov \| SCENE= }}
		+	===Crystal structure of FimH in complex with Heptylmannoside===
		+	{{ABSTRACT_PUBMED_24476493}}

-	~~The entry 4lov~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.

-	~~Authors~~: ~~Garcia-Pino, A~~.~~, Vanwetswinkel, S~~.~~, van Nuland, N~~.	+	==About this Structure==
		+	[[4lov]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LOV OCA].

-	~~Description~~: ~~Crystal structure of FimH in complex with Heptylmannoside~~	+	==Reference==
		+	<ref group="xtra">PMID:024476493</ref><references group="xtra"/><references/>
		+	[[Category: Garcia-Pino, A.]]
		+	[[Category: Nuland, N van.]]
		+	[[Category: Vanwetswinkel, S.]]
		+	[[Category: Carbohydrate binding protein]]
		+	[[Category: Ig fold]]
		+	[[Category: Pilus subunit]]

OCA at 20:13, 7 August 2013

2013-08-07T20:13:03Z

←Older revision		Revision as of 20:13, 7 August 2013
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	The entry 4lov is ON HOLD		The entry 4lov is ON HOLD

-	Authors: Garcia-Pino, A, Vanwetswinkel, S, van Nuland, N	+	Authors: Garcia-Pino, A., Vanwetswinkel, S., van Nuland, N.

	Description: Crystal structure of FimH in complex with Heptylmannoside		Description: Crystal structure of FimH in complex with Heptylmannoside

OCA: Protected "4lov" [edit=sysop:move=sysop]

2013-07-24T12:30:18Z

Protected "4lov" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:30, 24 July 2013

OCA: New page: '''Unreleased structure''' The entry 4lov is ON HOLD Authors: Garcia-Pino, A, Vanwetswinkel, S, van Nuland, N Description: Crystal structure of FimH in complex with Heptylmannoside

2013-07-24T12:30:16Z

New page: '''Unreleased structure''' The entry 4lov is ON HOLD Authors: Garcia-Pino, A, Vanwetswinkel, S, van Nuland, N Description: Crystal structure of FimH in complex with Heptylmannoside

New page

'''Unreleased structure'''

The entry 4lov is ON HOLD

Authors: Garcia-Pino, A, Vanwetswinkel, S, van Nuland, N

Description: Crystal structure of FimH in complex with Heptylmannoside