3mzk - Revision history

OCA at 10:27, 21 February 2024

OCA — Wed, 21 Feb 2024 10:27:15 GMT

←Older revision		Revision as of 10:27, 21 February 2024
Line 1:		Line 1:

	==Sec13/Sec16 complex, S.cerevisiae==		==Sec13/Sec16 complex, S.cerevisiae==
-	<StructureSection load='3mzk' size='340' side='right' caption='[[3mzk]], [[Resolution\|resolution]] 2.69Å' scene=''>	+	<StructureSection load='3mzk' size='340' side='right'caption='[[3mzk]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3mzk]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3MZK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3mzk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MZK FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[3mzl\|3mzl]]</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]] 2.69Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">ANU3, L8167~~.~~4, SEC13, YLR208W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=4932 ATCC 18824]), LPF1W, SEC16, YPL085W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])~~</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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [https://pdbe.org/3mzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [https://www.ebi.ac.uk/pdbsum/3mzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mzk ProSAT]</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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [~~http~~://pdbe.org/3mzk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3mzk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3mzk ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SEC13_YEAST SEC13_YEAST]] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.<ref>PMID:8565072</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:2188733</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9409822</ref> <ref>PMID:9199164</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:10747086</ref> <ref>PMID:11535824</ref> <ref>PMID:11717432</ref> <ref>PMID:12215173</ref> <ref>PMID:11823431</ref> <ref>PMID:12475940</ref> <ref>PMID:14627716</ref> <ref>PMID:21454883</ref> [[http://www.uniprot.org/uniprot/SEC16_YEAST SEC16_YEAST]] Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.<ref>PMID:7593161</ref> <ref>PMID:2188733</ref> <ref>PMID:7593162</ref> <ref>PMID:9325247</ref> <ref>PMID:9023343</ref> <ref>PMID:9880808</ref> <ref>PMID:10712514</ref> <ref>PMID:11694599</ref> <ref>PMID:12235121</ref>	+	[https://www.uniprot.org/uniprot/SEC13_YEAST SEC13_YEAST] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.<ref>PMID:8565072</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:2188733</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9409822</ref> <ref>PMID:9199164</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:10747086</ref> <ref>PMID:11535824</ref> <ref>PMID:11717432</ref> <ref>PMID:12215173</ref> <ref>PMID:11823431</ref> <ref>PMID:12475940</ref> <ref>PMID:14627716</ref> <ref>PMID:21454883</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mzk ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mzk ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-A resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1-ACE1 interface is observed both in the prior structure of Sec13-Sec31 and in Sec13-Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-A resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13-Sec31 coat.
-
-	Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.,Whittle JR, Schwartz TU J Cell Biol. 2010 Aug 9;190(3):347-61. PMID:20696705<ref>PMID:20696705</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3mzk" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 18824~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Schwartz, T U~~]]	+	[[Category: Saccharomyces cerevisiae]]
-	[[Category: ~~Whittle, J R~~]]	+	[[Category: Schwartz TU]]
-	[[Category: ~~Alpha-helical-stack]]~~	+	[[Category: Whittle JR]]
-	~~[[Category: Beta-propeller]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 13:45, 16 January 2019

OCA — Wed, 16 Jan 2019 13:45:05 GMT

←Older revision		Revision as of 13:45, 16 January 2019
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/3mzk_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/3mzk_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 08:22, 4 August 2016

OCA — Thu, 04 Aug 2016 08:22:26 GMT

←Older revision		Revision as of 08:22, 4 August 2016
Line 1:		Line 1:
		+
	==Sec13/Sec16 complex, S.cerevisiae==		==Sec13/Sec16 complex, S.cerevisiae==
	<StructureSection load='3mzk' size='340' side='right' caption='[[3mzk]], [[Resolution\|resolution]] 2.69Å' scene=''>		<StructureSection load='3mzk' size='340' side='right' caption='[[3mzk]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3mzk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae Saccharomyces cerevisiae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MZK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3mzk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MZK FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mzl\|3mzl]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mzl\|3mzl]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANU3, L8167.4, SEC13, YLR208W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ~~Saccharomyces cerevisiae~~]), LPF1W, SEC16, YPL085W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ~~Saccharomyces cerevisiae~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANU3, L8167.4, SEC13, YLR208W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), LPF1W, SEC16, YPL085W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [http://www.ebi.ac.uk/pdbsum/3mzk 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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [http://pdbe.org/3mzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [http://www.ebi.ac.uk/pdbsum/3mzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mzk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mzk ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	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 3mzk" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae~~]]	+	[[Category: Atcc 18824]]
	[[Category: Schwartz, T U]]		[[Category: Schwartz, T U]]
	[[Category: Whittle, J R]]		[[Category: Whittle, J R]]

OCA at 07:18, 25 December 2014

OCA — Thu, 25 Dec 2014 07:18:09 GMT

←Older revision		Revision as of 07:18, 25 December 2014
Line 7:		Line 7:
	<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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [http://www.ebi.ac.uk/pdbsum/3mzk 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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [http://www.ebi.ac.uk/pdbsum/3mzk PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SEC13_YEAST SEC13_YEAST]] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.<ref>PMID:8565072</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:2188733</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9409822</ref> <ref>PMID:9199164</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:10747086</ref> <ref>PMID:11535824</ref> <ref>PMID:11717432</ref> <ref>PMID:12215173</ref> <ref>PMID:11823431</ref> <ref>PMID:12475940</ref> <ref>PMID:14627716</ref> <ref>PMID:21454883</ref> [[http://www.uniprot.org/uniprot/SEC16_YEAST SEC16_YEAST]] Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.<ref>PMID:7593161</ref> <ref>PMID:2188733</ref> <ref>PMID:7593162</ref> <ref>PMID:9325247</ref> <ref>PMID:9023343</ref> <ref>PMID:9880808</ref> <ref>PMID:10712514</ref> <ref>PMID:11694599</ref> <ref>PMID:12235121</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 15:41, 18 December 2014

OCA — Thu, 18 Dec 2014 15:41:20 GMT

←Older revision		Revision as of 15:41, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3mzk~~\| ~~PDB~~=3mzk \| ~~SCENE~~= }}	+	==Sec13/Sec16 complex, S.cerevisiae==
-	===~~Sec13~~/~~Sec16 complex~~, S.cerevisiae===	+	<StructureSection load='3mzk' size='340' side='right' caption='[[3mzk]], [[Resolution\|resolution]] 2.69Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20696705}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3mzk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MZK FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mzl\|3mzl]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANU3, L8167.4, SEC13, YLR208W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), LPF1W, SEC16, YPL085W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [http://www.ebi.ac.uk/pdbsum/3mzk PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/3mzk_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-A resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1-ACE1 interface is observed both in the prior structure of Sec13-Sec31 and in Sec13-Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-A resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13-Sec31 coat.

-	~~==Function==~~	+	Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.,Whittle JR, Schwartz TU J Cell Biol. 2010 Aug 9;190(3):347-61. PMID:20696705<ref>PMID:20696705</ref>
-	~~[[http://www.uniprot.org/uniprot/SEC13_YEAST SEC13_YEAST]] Functions as a component~~ of the ~~nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double~~-~~membrane transport vesicle formation. First the small GTPase SAR1~~, ~~activated by and binding to the integral ER membrane protein SEC12, exchanges GDP~~ for ~~GTP and recruits~~ the ~~heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of~~ COPII coat ~~complexes then causes physically the deformation (budding) of the membrane~~, ~~leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein~~, ~~whose activity is stimulated in the presence of SEC13/31~~. ~~SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex~~ (~~NPC~~). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.<ref>PMID:8565072</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:2188733</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9409822</ref> <ref>PMID:9199164</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:10747086</ref> <ref>PMID:11535824</ref> <ref>PMID:11717432</ref> <ref>PMID:12215173</ref> <ref>PMID:11823431</ref> <ref>PMID:12475940</ref> <ref>PMID:14627716</ref> <ref>PMID:21454883</ref> [[http://www.uniprot.org/uniprot/SEC16_YEAST SEC16_YEAST]] Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.<ref>PMID:~~7593161</ref> <ref>PMID:2188733</ref> <ref>PMID:7593162</ref> <ref>PMID:9325247</ref> <ref>PMID:9023343</ref> <ref>PMID:9880808</ref> <ref>PMID:10712514</ref> <ref>PMID:11694599</ref>~~ <ref>PMID:~~12235121~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3mzk]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020696705</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	[[Category: Schwartz, T U.]]	+	[[Category: Schwartz, T U]]
-	[[Category: Whittle, J R.]]	+	[[Category: Whittle, J R]]
	[[Category: Alpha-helical-stack]]		[[Category: Alpha-helical-stack]]
	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]
	[[Category: Protein transport]]		[[Category: Protein transport]]

OCA: Protected "3mzk" [edit=sysop:move=sysop]

OCA — Wed, 17 Apr 2013 21:13:14 GMT

Protected "3mzk" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:13, 17 April 2013

OCA at 21:13, 17 April 2013

OCA — Wed, 17 Apr 2013 21:13:04 GMT

←Older revision		Revision as of 21:13, 17 April 2013
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-	{{Seed}}
-	[[Image:3mzk.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3mzk", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3mzk\| PDB=3mzk \| SCENE= }}		{{STRUCTURE_3mzk\| PDB=3mzk \| SCENE= }}
-
	===Sec13/Sec16 complex, S.cerevisiae===		===Sec13/Sec16 complex, S.cerevisiae===
		+	{{ABSTRACT_PUBMED_20696705}}

-		+	==Function==
-	<!--	+	[[http://www.uniprot.org/uniprot/SEC13_YEAST SEC13_YEAST]] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.<ref>PMID:8565072</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:2188733</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9409822</ref> <ref>PMID:9199164</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:10747086</ref> <ref>PMID:11535824</ref> <ref>PMID:11717432</ref> <ref>PMID:12215173</ref> <ref>PMID:11823431</ref> <ref>PMID:12475940</ref> <ref>PMID:14627716</ref> <ref>PMID:21454883</ref> [[http://www.uniprot.org/uniprot/SEC16_YEAST SEC16_YEAST]] Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.<ref>PMID:7593161</ref> <ref>PMID:2188733</ref> <ref>PMID:7593162</ref> <ref>PMID:9325247</ref> <ref>PMID:9023343</ref> <ref>PMID:9880808</ref> <ref>PMID:10712514</ref> <ref>PMID:11694599</ref> <ref>PMID:12235121</ref>
-	The ~~line below this paragraph~~, ~~{{ABSTRACT_PUBMED_20696705}}, adds~~ the ~~Publication Abstract~~ to the ~~page~~	+
-	(as ~~it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~)~~, where 20696705 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20696705}}~~	+

	==About this Structure==		==About this Structure==
-	~~3MZK~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA].	+	[[3mzk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20696705~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020696705</ref><references group="xtra"/><references/>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Schwartz, T U.]]		[[Category: Schwartz, T U.]]
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	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]
	[[Category: Protein transport]]		[[Category: Protein transport]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:46:36 2010''

OCA at 07:39, 18 August 2010

OCA — Wed, 18 Aug 2010 07:39:04 GMT

←Older revision		Revision as of 07:39, 18 August 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3mzk.jpg\|left\|200px]]

-	The ~~entry 3mzk~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3mzk", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3mzk\| PDB=3mzk \| SCENE= }}

-	~~Authors: Whittle~~, ~~J.R., Schwartz, T.U~~.	+	===Sec13/Sec16 complex, S.cerevisiae===

-	Description: Sec13/Sec16 complex, S.cerevisiae

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jun 16 08~~:28:33 2010''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20696705}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20696705 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20696705}}
		+
		+	==About this Structure==
		+	3MZK is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZK OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20696705</ref><references group="xtra"/>
		+	[[Category: Saccharomyces cerevisiae]]
		+	[[Category: Schwartz, T U.]]
		+	[[Category: Whittle, J R.]]
		+	[[Category: Alpha-helical-stack]]
		+	[[Category: Beta-propeller]]
		+	[[Category: Protein transport]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:46:36 2010''

OCA at 04:23, 16 June 2010

OCA — Wed, 16 Jun 2010 04:23:32 GMT

←Older revision		Revision as of 04:23, 16 June 2010
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3mzk is ON HOLD	+	The entry 3mzk is ON HOLD until Paper Publication

	Authors: Whittle, J.R., Schwartz, T.U.		Authors: Whittle, J.R., Schwartz, T.U.
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	Description: Sec13/Sec16 complex, S.cerevisiae		Description: Sec13/Sec16 complex, S.cerevisiae

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu May 20 09~~:19:59 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 16 08:28:33 2010''

OCA: New page: '''Unreleased structure''' The entry 3mzk is ON HOLD Authors: Whittle, J.R., Schwartz, T.U. Description: Sec13/Sec16 complex, S.cerevisiae ''Page seeded by [http://oca.weizmann.ac.il/...

OCA — Thu, 20 May 2010 06:20:00 GMT

New page: '''Unreleased structure''' The entry 3mzk is ON HOLD Authors: Whittle, J.R., Schwartz, T.U. Description: Sec13/Sec16 complex, S.cerevisiae ''Page seeded by [http://oca.weizmann.ac.il/...

New page

'''Unreleased structure'''

The entry 3mzk is ON HOLD

Authors: Whittle, J.R., Schwartz, T.U.

Description: Sec13/Sec16 complex, S.cerevisiae

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:19:59 2010''