5h72 - Revision history

OCA at 09:15, 20 March 2024

OCA — Wed, 20 Mar 2024 09:15:21 GMT

←Older revision		Revision as of 09:15, 20 March 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q9WZG2_THEMA Q9WZG2_THEMA] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069]		[https://www.uniprot.org/uniprot/Q9WZG2_THEMA Q9WZG2_THEMA] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The bacterial flagellar type III export apparatus, which is required for flagellar assembly beyond the cell membranes, consists of a transmembrane export gate complex and a cytoplasmic ATPase complex. FlhA, FlhB, FliP, FliQ, and FliR form the gate complex inside the basal body MS ring, although FliO is required for efficient export gate formation in Salmonella enterica. However, it remains unknown how they form the gate complex. Here we report that FliP forms a homohexameric ring with a diameter of 10 nm. Alanine substitutions of conserved Phe-137, Phe-150, and Glu-178 residues in the periplasmic domain of FliP (FliPP) inhibited FliP6 ring formation, suppressing flagellar protein export. FliO formed a 5-nm ring structure with 3 clamp-like structures that bind to the FliP6 ring. The crystal structure of FliPP derived from Thermotoga maritia, and structure-based photo-crosslinking experiments revealed that Phe-150 and Ser-156 of FliPP are involved in the FliP-FliP interactions and that Phe-150, Arg-152, Ser-156, and Pro-158 are responsible for the FliP-FliO interactions. Overexpression of FliP restored motility of a fliO mutant to the wild-type level, suggesting that the FliP6 ring is a functional unit in the export gate complex and that FliO is not part of the final gate structure. Copurification assays revealed that FlhA, FlhB, FliQ, and FliR are associated with the FliO/FliP complex. We propose that the assembly of the export gate complex begins with FliP6 ring formation with the help of the FliO scaffold, followed by FliQ, FliR, and FlhB and finally FlhA during MS ring formation.
-
-	Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.,Fukumura T, Makino F, Dietsche T, Kinoshita M, Kato T, Wagner S, Namba K, Imada K, Minamino T PLoS Biol. 2017 Aug 3;15(8):e2002281. doi: 10.1371/journal.pbio.2002281., eCollection 2017 Aug. PMID:28771466<ref>PMID:28771466</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5h72" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Flagellar protein 3D structures\|Flagellar protein 3D structures]]		*[[Flagellar protein 3D structures\|Flagellar protein 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:25, 9 August 2023

OCA — Wed, 09 Aug 2023 07:25:53 GMT

←Older revision		Revision as of 07:25, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='5h72' size='340' side='right'caption='[[5h72]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='5h72' size='340' side='right'caption='[[5h72]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h72]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H72 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5H72 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h72]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H72 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h72 OCA], [~~http~~://pdbe.org/5h72 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5h72 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5h72 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5h72 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]] 2.4Å</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=5h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h72 OCA], [https://pdbe.org/5h72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h72 RCSB], [https://www.ebi.ac.uk/pdbsum/5h72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h72 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/Q9WZG2_THEMA Q9WZG2_THEMA]] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069]	+	[https://www.uniprot.org/uniprot/Q9WZG2_THEMA Q9WZG2_THEMA] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fukumura, T]]	+	[[Category: Thermotoga maritima MSB8]]
-	[[Category: Imada, K]]	+	[[Category: Fukumura T]]
-	[[Category: Kawaguchi, T]]	+	[[Category: Imada K]]
-	[[Category: Minamino, T]]	+	[[Category: Kawaguchi T]]
-	[[Category: Namba, K]]	+	[[Category: Minamino T]]
-	[[Category: Saijo-Hamano, Y]]	+	[[Category: Namba K]]
-	~~[[Category: Biosynthetic protein]]~~	+	[[Category: Saijo-Hamano Y]]
-	~~[[Category: Flagellar protein export~~]]	+

OCA at 06:54, 20 May 2020

OCA — Wed, 20 May 2020 06:54:16 GMT

←Older revision		Revision as of 06:54, 20 May 2020
Line 1:		Line 1:

	==Structure of the periplasmic domain of FliP==		==Structure of the periplasmic domain of FliP==
-	<StructureSection load='5h72' size='340' side='right' caption='[[5h72]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='5h72' size='340' side='right'caption='[[5h72]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h72]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H72 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5H72 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h72]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H72 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H72 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=5h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h72 OCA], [http://pdbe.org/5h72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h72 RCSB], [http://www.ebi.ac.uk/pdbsum/5h72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h72 ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h72 OCA], [http://pdbe.org/5h72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h72 RCSB], [http://www.ebi.ac.uk/pdbsum/5h72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h72 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 5h72" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5h72" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Flagellar protein 3D structures\|Flagellar protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Fukumura, T]]		[[Category: Fukumura, T]]
	[[Category: Imada, K]]		[[Category: Imada, K]]

OCA at 03:55, 30 August 2017

OCA — Wed, 30 Aug 2017 03:55:23 GMT

←Older revision		Revision as of 03:55, 30 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5h72 is ~~ON HOLD until Paper~~ Publication	+	==Structure of the periplasmic domain of FliP==
		+	<StructureSection load='5h72' size='340' side='right' caption='[[5h72]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5h72]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H72 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H72 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=5h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h72 OCA], [http://pdbe.org/5h72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h72 RCSB], [http://www.ebi.ac.uk/pdbsum/5h72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h72 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q9WZG2_THEMA Q9WZG2_THEMA]] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The bacterial flagellar type III export apparatus, which is required for flagellar assembly beyond the cell membranes, consists of a transmembrane export gate complex and a cytoplasmic ATPase complex. FlhA, FlhB, FliP, FliQ, and FliR form the gate complex inside the basal body MS ring, although FliO is required for efficient export gate formation in Salmonella enterica. However, it remains unknown how they form the gate complex. Here we report that FliP forms a homohexameric ring with a diameter of 10 nm. Alanine substitutions of conserved Phe-137, Phe-150, and Glu-178 residues in the periplasmic domain of FliP (FliPP) inhibited FliP6 ring formation, suppressing flagellar protein export. FliO formed a 5-nm ring structure with 3 clamp-like structures that bind to the FliP6 ring. The crystal structure of FliPP derived from Thermotoga maritia, and structure-based photo-crosslinking experiments revealed that Phe-150 and Ser-156 of FliPP are involved in the FliP-FliP interactions and that Phe-150, Arg-152, Ser-156, and Pro-158 are responsible for the FliP-FliO interactions. Overexpression of FliP restored motility of a fliO mutant to the wild-type level, suggesting that the FliP6 ring is a functional unit in the export gate complex and that FliO is not part of the final gate structure. Copurification assays revealed that FlhA, FlhB, FliQ, and FliR are associated with the FliO/FliP complex. We propose that the assembly of the export gate complex begins with FliP6 ring formation with the help of the FliO scaffold, followed by FliQ, FliR, and FlhB and finally FlhA during MS ring formation.

-	~~Authors~~:	+	Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.,Fukumura T, Makino F, Dietsche T, Kinoshita M, Kato T, Wagner S, Namba K, Imada K, Minamino T PLoS Biol. 2017 Aug 3;15(8):e2002281. doi: 10.1371/journal.pbio.2002281., eCollection 2017 Aug. PMID:28771466<ref>PMID:28771466</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5h72" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Fukumura, T]]
		+	[[Category: Imada, K]]
		+	[[Category: Kawaguchi, T]]
		+	[[Category: Minamino, T]]
		+	[[Category: Namba, K]]
		+	[[Category: Saijo-Hamano, Y]]
		+	[[Category: Biosynthetic protein]]
		+	[[Category: Flagellar protein export]]

OCA at 07:04, 4 May 2017

OCA — Thu, 04 May 2017 07:04:21 GMT

←Older revision		Revision as of 07:04, 4 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5h72 is ON HOLD	+	The entry 5h72 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5h72" [edit=sysop:move=sysop]

OCA — Fri, 09 Dec 2016 13:49:40 GMT

Protected "5h72" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:49, 9 December 2016

OCA: New page: '''Unreleased structure''' The entry 5h72 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Fri, 09 Dec 2016 13:49:38 GMT

New page: '''Unreleased structure''' The entry 5h72 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5h72 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]