6kmv - Revision history

OCA at 10:37, 22 November 2023

OCA — Wed, 22 Nov 2023 10:37:28 GMT

←Older revision		Revision as of 10:37, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='6kmv' size='340' side='right'caption='[[6kmv]], [[Resolution\|resolution]] 3.35Å' scene=''>		<StructureSection load='6kmv' size='340' side='right'caption='[[6kmv]], [[Resolution\|resolution]] 3.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6kmv]] is a 48 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6KMV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6kmv]] is a 29 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KMV FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[6kmu\|6kmu]]</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]] 3.35Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">Casp4, Casp11, Caspl, Ich3 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=10090 LK3 transgenic mice]), Gsdmdc1, Gsdmd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6kmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmv OCA], [https://pdbe.org/6kmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kmv RCSB], [https://www.ebi.ac.uk/pdbsum/6kmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmv ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-11 Caspase-11], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.64 3.4.22.64] </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=6kmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmv OCA], [~~http~~://pdbe.org/6kmv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6kmv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6kmv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmv ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/GSDMD_MOUSE GSDMD_MOUSE]] Gasdermin-D, N-terminal: Promotes pyroptosis in response to microbial infection and danger signals. Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1 or CASP4 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators (PubMed:26611636, PubMed:26375259, PubMed:26375003, PubMed:27418190, PubMed:27385778, PubMed:27383986). After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids, including monophosphorylated phosphatidylinositols, such as phosphatidylinositol 4-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-trisphosphate, and more weakly to phosphatidic acid and phosphatidylserine. Homooligomerizes within the membrane and forms pores of 10 - 15 nanometers (nm) of inner diameter, allowing the release of mature IL1B and triggering pyroptosis. Exhibits bactericidal activity. Gasdermin-D, N-terminal released from pyroptotic cells into the extracellular milieu rapidly binds to and kills both Gram-negative and Gram-positive bacteria, without harming neighboring mammalian cells, as it does not disrupt the plasma membrane from the outside due to lipid-binding specificity. Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes. Strongly binds to bacterial and mitochondrial lipids, including cardiolipin. Does not bind to phosphatidylethanolamine or phosphatidylcholine (PubMed:27383986).<ref>PMID:26375003</ref> <ref>PMID:26375259</ref> <ref>PMID:26611636</ref> <ref>PMID:27383986</ref> <ref>PMID:27385778</ref> <ref>PMID:27418190</ref> [[http://www.uniprot.org/uniprot/CASP4_MOUSE CASP4_MOUSE]] Proinflammatory caspase (PubMed:8702803, PubMed:9038361, PubMed:25119034). Essential effector of NLRP3 inflammasome-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS, as well as infection with Gram-negative bacteria (PubMed:22002608). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:22002608, PubMed:26320999, PubMed:26375003). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection. In later stages of the infection (>3 days post infection), LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in the pyroptosis of the infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (PubMed:25121752). Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (By similarity). Involved in cell death induced by endoplasmic reticulum stress (By similarity). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Does not directly process IL1B (PubMed:8702803, PubMed:9038361). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590).[UniProtKB:P49662]<ref>PMID:22002608</ref> <ref>PMID:25119034</ref> <ref>PMID:25121752</ref> <ref>PMID:26320999</ref> <ref>PMID:26375003</ref> <ref>PMID:28314590</ref> <ref>PMID:8702803</ref> <ref>PMID:9038361</ref>	+	[https://www.uniprot.org/uniprot/CASP4_MOUSE CASP4_MOUSE] Proinflammatory caspase (PubMed:8702803, PubMed:9038361, PubMed:25119034). Essential effector of NLRP3 inflammasome-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS, as well as infection with Gram-negative bacteria (PubMed:22002608). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:22002608, PubMed:26320999, PubMed:26375003). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection. In later stages of the infection (>3 days post infection), LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in the pyroptosis of the infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (PubMed:25121752). Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (By similarity). Involved in cell death induced by endoplasmic reticulum stress (By similarity). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Does not directly process IL1B (PubMed:8702803, PubMed:9038361). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590).[UniProtKB:P49662]<ref>PMID:22002608</ref> <ref>PMID:25119034</ref> <ref>PMID:25121752</ref> <ref>PMID:26320999</ref> <ref>PMID:26375003</ref> <ref>PMID:28314590</ref> <ref>PMID:8702803</ref> <ref>PMID:9038361</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 6kmv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6kmv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Caspase 3D structures\|Caspase 3D structures]]
		+	*[[Gasdermin 3D structures\|Gasdermin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Caspase-11]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Ding, J]]	+	[[Category: Ding J]]
-	[[Category: Sun, Q]]	+	[[Category: Sun Q]]
-	~~[[Category: Immune system]]~~	+
-	~~[[Category: Pyroptosis~~]]	+

OCA at 10:35, 27 March 2020

OCA — Fri, 27 Mar 2020 10:35:23 GMT

←Older revision		Revision as of 10:35, 27 March 2020
Line 3:		Line 3:
	<StructureSection load='6kmv' size='340' side='right'caption='[[6kmv]], [[Resolution\|resolution]] 3.35Å' scene=''>		<StructureSection load='6kmv' size='340' side='right'caption='[[6kmv]], [[Resolution\|resolution]] 3.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6kmv]] is a 48 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KMV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6kmv]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KMV FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6kmu\|6kmu]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6kmu\|6kmu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Casp4, Casp11, Caspl, Ich3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Gsdmdc1, Gsdmd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-11 Caspase-11], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.64 3.4.22.64] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-11 Caspase-11], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.64 3.4.22.64] </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=6kmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmv OCA], [http://pdbe.org/6kmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kmv RCSB], [http://www.ebi.ac.uk/pdbsum/6kmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmv 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=6kmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmv OCA], [http://pdbe.org/6kmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kmv RCSB], [http://www.ebi.ac.uk/pdbsum/6kmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmv ProSAT]</span></td></tr>
Line 25:		Line 26:
	[[Category: Caspase-11]]		[[Category: Caspase-11]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Ding, J]]		[[Category: Ding, J]]
	[[Category: Sun, Q]]		[[Category: Sun, Q]]
	[[Category: Immune system]]		[[Category: Immune system]]
	[[Category: Pyroptosis]]		[[Category: Pyroptosis]]

OCA at 07:17, 11 March 2020

OCA — Wed, 11 Mar 2020 07:17:45 GMT

←Older revision		Revision as of 07:17, 11 March 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6kmv is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==caspase-11 C254A P22/P10 in complex with mouse GSDMD-C domain==
		+	<StructureSection load='6kmv' size='340' side='right'caption='[[6kmv]], [[Resolution\|resolution]] 3.35Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6kmv]] is a 48 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KMV FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6kmu\|6kmu]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-11 Caspase-11], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.64 3.4.22.64] </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=6kmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmv OCA], [http://pdbe.org/6kmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kmv RCSB], [http://www.ebi.ac.uk/pdbsum/6kmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmv ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GSDMD_MOUSE GSDMD_MOUSE]] Gasdermin-D, N-terminal: Promotes pyroptosis in response to microbial infection and danger signals. Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1 or CASP4 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators (PubMed:26611636, PubMed:26375259, PubMed:26375003, PubMed:27418190, PubMed:27385778, PubMed:27383986). After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids, including monophosphorylated phosphatidylinositols, such as phosphatidylinositol 4-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-trisphosphate, and more weakly to phosphatidic acid and phosphatidylserine. Homooligomerizes within the membrane and forms pores of 10 - 15 nanometers (nm) of inner diameter, allowing the release of mature IL1B and triggering pyroptosis. Exhibits bactericidal activity. Gasdermin-D, N-terminal released from pyroptotic cells into the extracellular milieu rapidly binds to and kills both Gram-negative and Gram-positive bacteria, without harming neighboring mammalian cells, as it does not disrupt the plasma membrane from the outside due to lipid-binding specificity. Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes. Strongly binds to bacterial and mitochondrial lipids, including cardiolipin. Does not bind to phosphatidylethanolamine or phosphatidylcholine (PubMed:27383986).<ref>PMID:26375003</ref> <ref>PMID:26375259</ref> <ref>PMID:26611636</ref> <ref>PMID:27383986</ref> <ref>PMID:27385778</ref> <ref>PMID:27418190</ref> [[http://www.uniprot.org/uniprot/CASP4_MOUSE CASP4_MOUSE]] Proinflammatory caspase (PubMed:8702803, PubMed:9038361, PubMed:25119034). Essential effector of NLRP3 inflammasome-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS, as well as infection with Gram-negative bacteria (PubMed:22002608). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:22002608, PubMed:26320999, PubMed:26375003). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection. In later stages of the infection (>3 days post infection), LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in the pyroptosis of the infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (PubMed:25121752). Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (By similarity). Involved in cell death induced by endoplasmic reticulum stress (By similarity). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Does not directly process IL1B (PubMed:8702803, PubMed:9038361). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590).[UniProtKB:P49662]<ref>PMID:22002608</ref> <ref>PMID:25119034</ref> <ref>PMID:25121752</ref> <ref>PMID:26320999</ref> <ref>PMID:26375003</ref> <ref>PMID:28314590</ref> <ref>PMID:8702803</ref> <ref>PMID:9038361</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The pyroptosis execution protein GSDMD is cleaved by inflammasome-activated caspase-1 and LPS-activated caspase-11/4/5. The cleavage unmasks the pore-forming domain from GSDMD-C-terminal domain. How the caspases recognize GSDMD and its connection with caspase activation are unknown. Here, we show site-specific caspase-4/11 autoprocessing, generating a p10 product, is required and sufficient for cleaving GSDMD and inducing pyroptosis. The p10-form autoprocessed caspase-4/11 binds the GSDMD-C domain with a high affinity. Structural comparison of autoprocessed and unprocessed capase-11 identifies a beta sheet induced by the autoprocessing. In caspase-4/11-GSDMD-C complex crystal structures, the beta sheet organizes a hydrophobic GSDMD-binding interface that is only possible for p10-form caspase-4/11. The binding promotes dimerization-mediated caspase activation, rendering a cleavage independently of the cleavage-site tetrapeptide sequence. Crystal structure of caspase-1-GSDMD-C complex shows a similar GSDMD-recognition mode. Our study reveals an unprecedented substrate-targeting mechanism for caspases. The hydrophobic interface suggests an additional space for developing inhibitors specific for pyroptotic caspases.

-	~~Authors~~:	+	Structural Mechanism for GSDMD Targeting by Autoprocessed Caspases in Pyroptosis.,Wang K, Sun Q, Zhong X, Zeng M, Zeng H, Shi X, Li Z, Wang Y, Zhao Q, Shao F, Ding J Cell. 2020 Mar 5;180(5):941-955.e20. doi: 10.1016/j.cell.2020.02.002. Epub 2020, Feb 27. PMID:32109412<ref>PMID:32109412</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6kmv" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Caspase-11]]
		+	[[Category: Large Structures]]
		+	[[Category: Ding, J]]
		+	[[Category: Sun, Q]]
		+	[[Category: Immune system]]
		+	[[Category: Pyroptosis]]

OCA at 06:34, 2 October 2019

OCA — Wed, 02 Oct 2019 06:34:50 GMT

←Older revision		Revision as of 06:34, 2 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 07 Aug 2019 04:12:51 GMT

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

←Older revision

Revision as of 04:12, 7 August 2019

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

OCA — Wed, 07 Aug 2019 04:12:49 GMT

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

New page

'''Unreleased structure'''

The entry 6kmv is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]