6tz9 - Revision history

OCA at 09:28, 20 March 2024

OCA — Wed, 20 Mar 2024 09:28:15 GMT

←Older revision		Revision as of 09:28, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='6tz9' size='340' side='right'caption='[[6tz9]], [[Resolution\|resolution]] 6.20Å' scene=''>		<StructureSection load='6tz9' size='340' side='right'caption='[[6tz9]], [[Resolution\|resolution]] 6.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6tz9]] is a 26 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZ9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6TZ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tz9]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TZ9 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CHMP1B~~, ~~C18orf2 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 6.2Å</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=6tz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tz9 OCA], [~~http~~://pdbe.org/6tz9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6tz9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6tz9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6tz9 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=6tz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tz9 OCA], [https://pdbe.org/6tz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tz9 RCSB], [https://www.ebi.ac.uk/pdbsum/6tz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tz9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_HUMAN]] Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>	+	[https://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_HUMAN] Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The endosomal sorting complexes required for transport (ESCRTs) mediate diverse membrane remodeling events. These typically require ESCRT-III proteins to stabilize negatively curved membranes; however, recent work has indicated that certain ESCRT-IIIs also participate in positive-curvature membrane-shaping reactions. ESCRT-IIIs polymerize into membrane-binding filaments, but the structural basis for negative versus positive membrane remodeling by these proteins remains poorly understood. To learn how certain ESCRT-IIIs shape positively curved membranes, we determined structures of human membrane-bound CHMP1B-only, membrane-bound CHMP1B + IST1, and IST1-only filaments by cryo-EM. Our structures show how CHMP1B first polymerizes into a single-stranded helical filament, shaping membranes into moderate-curvature tubules. Subsequently, IST1 assembles a second strand on CHMP1B, further constricting the membrane tube and reducing its diameter nearly to the fission point. Each step of constriction thins the underlying bilayer, lowering the barrier to membrane fission. Our structures reveal how a two-component, sequential polymerization mechanism drives membrane tubulation, constriction and bilayer thinning.	+

-	Membrane constriction and thinning by sequential ESCRT-III polymerization.,Nguyen HC, Talledge N, McCullough J, Sharma A, Moss FR 3rd, Iwasa JH, Vershinin MD, Sundquist WI, Frost A Nat Struct Mol Biol. 2020 Apr;27(4):392-399. doi: 10.1038/s41594-020-0404-x. Epub, 2020 Apr 6. PMID:32251413<ref>PMID:32251413</ref>	+	==See Also==
-		+	*[[Charged multivesicular body protein 3D structures\|Charged multivesicular body protein 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+	*[[Vacuolar protein sorting-associated protein 3D structures\|Vacuolar protein sorting-associated protein 3D structures]]
-	~~</div>~~	+
-	~~<div class="pdbe~~-~~citations 6tz9" style="background~~-~~color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Frost, A]]	+	[[Category: Frost A]]
-	[[Category: Nguyen~~, H C]]~~	+	[[Category: Nguyen HC]]
-	~~[[Category: Escrt-iii]]~~	+
-	~~[[Category: Lipid binding protein]]~~	+
-	~~[[Category: Membrane remodeling]]~~	+
-	~~[[Category: Membrane-bound protein filament~~]]	+

OCA at 06:08, 22 April 2020

OCA — Wed, 22 Apr 2020 06:08:33 GMT

←Older revision		Revision as of 06:08, 22 April 2020
Line 3:		Line 3:
	<StructureSection load='6tz9' size='340' side='right'caption='[[6tz9]], [[Resolution\|resolution]] 6.20Å' scene=''>		<StructureSection load='6tz9' size='340' side='right'caption='[[6tz9]], [[Resolution\|resolution]] 6.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6tz9]] is a 26 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TZ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tz9]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TZ9 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=6tz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tz9 OCA], [http://pdbe.org/6tz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tz9 RCSB], [http://www.ebi.ac.uk/pdbsum/6tz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tz9 ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CHMP1B, C18orf2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6tz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tz9 OCA], [http://pdbe.org/6tz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tz9 RCSB], [http://www.ebi.ac.uk/pdbsum/6tz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tz9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_HUMAN]] Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>		[[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_HUMAN]] Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The endosomal sorting complexes required for transport (ESCRTs) mediate diverse membrane remodeling events. These typically require ESCRT-III proteins to stabilize negatively curved membranes; however, recent work has indicated that certain ESCRT-IIIs also participate in positive-curvature membrane-shaping reactions. ESCRT-IIIs polymerize into membrane-binding filaments, but the structural basis for negative versus positive membrane remodeling by these proteins remains poorly understood. To learn how certain ESCRT-IIIs shape positively curved membranes, we determined structures of human membrane-bound CHMP1B-only, membrane-bound CHMP1B + IST1, and IST1-only filaments by cryo-EM. Our structures show how CHMP1B first polymerizes into a single-stranded helical filament, shaping membranes into moderate-curvature tubules. Subsequently, IST1 assembles a second strand on CHMP1B, further constricting the membrane tube and reducing its diameter nearly to the fission point. Each step of constriction thins the underlying bilayer, lowering the barrier to membrane fission. Our structures reveal how a two-component, sequential polymerization mechanism drives membrane tubulation, constriction and bilayer thinning.
		+
		+	Membrane constriction and thinning by sequential ESCRT-III polymerization.,Nguyen HC, Talledge N, McCullough J, Sharma A, Moss FR 3rd, Iwasa JH, Vershinin MD, Sundquist WI, Frost A Nat Struct Mol Biol. 2020 Apr;27(4):392-399. doi: 10.1038/s41594-020-0404-x. Epub, 2020 Apr 6. PMID:32251413<ref>PMID:32251413</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6tz9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Frost, A]]		[[Category: Frost, A]]

OCA at 06:56, 8 April 2020

OCA — Wed, 08 Apr 2020 06:56:50 GMT

←Older revision		Revision as of 06:56, 8 April 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6tz9 is ~~ON HOLD~~ ~~until Paper Publication~~	+	==CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only==
-		+	<StructureSection load='6tz9' size='340' side='right'caption='[[6tz9]], [[Resolution\|resolution]] 6.20Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6tz9]] is a 26 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TZ9 FirstGlance]. <br>
-	~~Description~~:	+	</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=6tz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tz9 OCA], [http://pdbe.org/6tz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tz9 RCSB], [http://www.ebi.ac.uk/pdbsum/6tz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tz9 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_HUMAN]] Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Frost, A]]
		+	[[Category: Nguyen, H C]]
		+	[[Category: Escrt-iii]]
		+	[[Category: Lipid binding protein]]
		+	[[Category: Membrane remodeling]]
		+	[[Category: Membrane-bound protein filament]]

OCA at 08:03, 2 October 2019

OCA — Wed, 02 Oct 2019 08:03:14 GMT

←Older revision		Revision as of 08:03, 2 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6tz9 is ON HOLD	+	The entry 6tz9 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6tz9" [edit=sysop:move=sysop]

OCA — Wed, 21 Aug 2019 04:24:55 GMT

Protected "6tz9" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:24, 21 August 2019

OCA: New page: '''Unreleased structure''' The entry 6tz9 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 21 Aug 2019 04:24:53 GMT

New page: '''Unreleased structure''' The entry 6tz9 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6tz9 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]