5khe - Revision history

OCA at 10:46, 27 September 2023

OCA — Wed, 27 Sep 2023 10:46:46 GMT

←Older revision		Revision as of 10:46, 27 September 2023
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	<SX load='5khe' size='340' side='right' viewer='molstar' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>		<SX load='5khe' size='340' side='right' viewer='molstar' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Rubv Rubv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5KHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rubella_virus Rubella virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KHE FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5khc\|5khc]]~~, [[~~5khf~~\|~~5khf~~]]</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]] 35Å</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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [~~http~~://pdbe.org/5khe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5khe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe 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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [https://pdbe.org/5khe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [https://www.ebi.ac.uk/pdbsum/5khe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/POLS_RUBVT POLS_RUBVT]] Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells (By similarity). E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein (By similarity). E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function (By similarity).	+	[https://www.uniprot.org/uniprot/POLS_RUBVT POLS_RUBVT] Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells (By similarity). E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein (By similarity). E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</SX>		</SX>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Rubv~~]]	+	[[Category: Rubella virus]]
-	[[Category: Klose, T]]	+	[[Category: Klose T]]
-	[[Category: Prasad, V ~~Mangala~~]]	+	[[Category: Mangala Prasad V]]
-	[[Category: Rossmann~~, M G]]~~	+	[[Category: Rossmann MG]]
-	~~[[Category: Rubella virus capsid protein]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 20:31, 10 April 2020

OCA — Fri, 10 Apr 2020 20:31:52 GMT

←Older revision		Revision as of 20:31, 10 April 2020
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	<SX load='5khe' size='340' side='right' viewer='molstar' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>		<SX load='5khe' size='340' side='right' viewer='molstar' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubv Rubv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5KHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubv Rubv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KHE FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5khc\|5khc]], [[5khf\|5khf]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5khc\|5khc]], [[5khf\|5khf]]</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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [http://pdbe.org/5khe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [http://www.ebi.ac.uk/pdbsum/5khe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe ProSAT]</span></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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [http://pdbe.org/5khe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [http://www.ebi.ac.uk/pdbsum/5khe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 18:48, 6 March 2020

OCA — Fri, 06 Mar 2020 18:48:24 GMT

←Older revision		Revision as of 18:48, 6 March 2020
Line 1:		Line 1:

	==Fitted structure of rubella virus capsid protein==		==Fitted structure of rubella virus capsid protein==
-	<~~StructureSection~~ load='5khe' size='340' side='right'caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>	+	<SX load='5khe' size='340' side='right' viewer='molstar' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubv Rubv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubv Rubv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHE FirstGlance]. <br>
Line 21:		Line 21:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Rubv]]		[[Category: Rubv]]

OCA at 16:28, 11 December 2019

OCA — Wed, 11 Dec 2019 16:28:15 GMT

←Older revision		Revision as of 16:28, 11 December 2019
Line 1:		Line 1:

	==Fitted structure of rubella virus capsid protein==		==Fitted structure of rubella virus capsid protein==
-	<StructureSection load='5khe' size='340' side='right' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>	+	<StructureSection load='5khe' size='340' side='right'caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubv Rubv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHE FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5khc\|5khc]], [[5khf\|5khf]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5khc\|5khc]], [[5khf\|5khf]]</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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [http://pdbe.org/5khe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [http://www.ebi.ac.uk/pdbsum/5khe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe 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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [http://pdbe.org/5khe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [http://www.ebi.ac.uk/pdbsum/5khe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe ProSAT]</span></td></tr>
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Rubv]]
	[[Category: Klose, T]]		[[Category: Klose, T]]
	[[Category: Prasad, V Mangala]]		[[Category: Prasad, V Mangala]]

OCA at 10:18, 3 August 2017

OCA — Thu, 03 Aug 2017 10:18:21 GMT

←Older revision		Revision as of 10:18, 3 August 2017
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/POLS_RUBVT POLS_RUBVT]] Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells (By similarity). E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein (By similarity). E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function (By similarity).		[[http://www.uniprot.org/uniprot/POLS_RUBVT POLS_RUBVT]] Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells (By similarity). E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein (By similarity). E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Viral infections during pregnancy are a significant cause of infant morbidity and mortality. Of these, rubella virus infection is a well-substantiated example that leads to miscarriages or severe fetal defects. However, structural information about the rubella virus has been lacking due to the pleomorphic nature of the virions. Here we report a helical structure of rubella virions using cryo-electron tomography. Sub-tomogram averaging of the surface spikes established the relative positions of the viral glycoproteins, which differed from the earlier icosahedral models of the virus. Tomographic analyses of in vitro assembled nucleocapsids and virions provide a template for viral assembly. Comparisons of immature and mature virions show large rearrangements in the glycoproteins that may be essential for forming the infectious virions. These results present the first known example of a helical membrane-enveloped virus, while also providing a structural basis for its assembly and maturation pathway.
		+
		+	Assembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.,Mangala Prasad V, Klose T, Rossmann MG PLoS Pathog. 2017 Jun 2;13(6):e1006377. doi: 10.1371/journal.ppat.1006377., eCollection 2017 Jun. PMID:28575072<ref>PMID:28575072</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5khe" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:57, 10 May 2017

OCA — Wed, 10 May 2017 12:57:22 GMT

←Older revision		Revision as of 12:57, 10 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5khe is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Fitted structure of rubella virus capsid protein==
-		+	<StructureSection load='5khe' size='340' side='right' caption='[[5khe]], [[Resolution\|resolution]] 35.00Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5khe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHE FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5khc\|5khc]], [[5khf\|5khf]]</td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=5khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khe OCA], [http://pdbe.org/5khe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khe RCSB], [http://www.ebi.ac.uk/pdbsum/5khe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khe ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLS_RUBVT POLS_RUBVT]] Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells (By similarity). E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein (By similarity). E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function (By similarity).
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Klose, T]]
		+	[[Category: Prasad, V Mangala]]
		+	[[Category: Rossmann, M G]]
		+	[[Category: Rubella virus capsid protein]]
		+	[[Category: Viral protein]]

OCA at 09:17, 14 July 2016

OCA — Thu, 14 Jul 2016 09:17:17 GMT

←Older revision		Revision as of 09:17, 14 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Thu, 23 Jun 2016 21:37:05 GMT

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

←Older revision

Revision as of 21:37, 23 June 2016

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

OCA — Thu, 23 Jun 2016 21:37:03 GMT

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

New page

'''Unreleased structure'''

The entry 5khe is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]