8a1d - Revision history

OCA at 16:47, 9 July 2025

2025-07-09T16:47:08Z

← Older revision		Revision as of 16:47, 9 July 2025
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8a1d]] is a 16 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=8A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1D FirstGlance]. <br>		<table><tr><td colspan='2'>[[8a1d]] is a 16 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=8A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1D FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 3Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=8a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1d OCA], [https://pdbe.org/8a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1d RCSB], [https://www.ebi.ac.uk/pdbsum/8a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1d 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=8a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1d OCA], [https://pdbe.org/8a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1d RCSB], [https://www.ebi.ac.uk/pdbsum/8a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/MPEG1_MOUSE MPEG1_MOUSE] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).<ref>PMID:23257510</ref> <ref>PMID:23753625</ref> <ref>PMID:26402460</ref> <ref>PMID:26831467</ref> <ref>PMID:30249808</ref>		[https://www.uniprot.org/uniprot/MPEG1_MOUSE MPEG1_MOUSE] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).<ref>PMID:23257510</ref> <ref>PMID:23753625</ref> <ref>PMID:26402460</ref> <ref>PMID:26831467</ref> <ref>PMID:30249808</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Perforin-2 (PFN2, MPEG1) is a key pore-forming protein in mammalian innate immunity restricting intracellular bacteria proliferation. It forms a membrane-bound pre-pore complex that converts to a pore-forming structure upon acidification; but its mechanism of conformational transition has been debated. Here we used cryo-electron microscopy, tomography and subtomogram averaging to determine structures of PFN2 in pre-pore and pore conformations in isolation and bound to liposomes. In isolation and upon acidification, the pre-assembled complete pre-pore rings convert to pores in both flat ring and twisted conformations. On membranes, in situ assembled PFN2 pre-pores display various degrees of completeness; whereas PFN2 pores are mainly incomplete arc structures that follow the same subunit packing arrangements as found in isolation. Both assemblies on membranes use their P2 beta-hairpin for binding to the lipid membrane surface. Overall, these structural snapshots suggest a molecular mechanism for PFN2 pre-pore to pore transition on a targeted membrane, potentially using the twisted pore as an intermediate or alternative state to the flat conformation, with the capacity to cause bilayer distortion during membrane insertion.

			Cryo-EM structures of perforin-2 in isolation and assembled on a membrane suggest a mechanism for pore formation.,Yu X, Ni T, Munson G, Zhang P, Gilbert RJC EMBO J. 2022 Dec 1;41(23):e111857. doi: 10.15252/embj.2022111857. Epub 2022 Oct , 17. PMID:36245269<ref>PMID:36245269</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 8a1d" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:30, 24 November 2022

2022-11-24T10:30:17Z

← Older revision		Revision as of 10:30, 24 November 2022
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	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MPEG1_MOUSE MPEG1_MOUSE]] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).<ref>PMID:23257510</ref> <ref>PMID:23753625</ref> <ref>PMID:26402460</ref> <ref>PMID:26831467</ref> <ref>PMID:30249808</ref>		[https://www.uniprot.org/uniprot/MPEG1_MOUSE MPEG1_MOUSE] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).<ref>PMID:23257510</ref> <ref>PMID:23753625</ref> <ref>PMID:26402460</ref> <ref>PMID:26831467</ref> <ref>PMID:30249808</ref>
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:06, 8 September 2022

2022-09-08T05:06:20Z

← Older revision		Revision as of 05:06, 8 September 2022
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	==Structure of murine perforin-2 (Mpeg1) pore in ring form==		==Structure of murine perforin-2 (Mpeg1) pore in ring form==
	<StructureSection load='8a1d' size='340' side='right'caption='[[8a1d]]' scene=''>		<StructureSection load='8a1d' size='340' side='right'caption='[[8a1d]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1D FirstGlance]. <br>		<table><tr><td colspan='2'>[[8a1d]] is a 16 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=8A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1D FirstGlance]. <br>
	</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=8a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1d OCA], [https://pdbe.org/8a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1d RCSB], [https://www.ebi.ac.uk/pdbsum/8a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1d ProSAT]</span></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=8a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1d OCA], [https://pdbe.org/8a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1d RCSB], [https://www.ebi.ac.uk/pdbsum/8a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1d ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[[https://www.uniprot.org/uniprot/MPEG1_MOUSE MPEG1_MOUSE]] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).<ref>PMID:23257510</ref> <ref>PMID:23753625</ref> <ref>PMID:26402460</ref> <ref>PMID:26831467</ref> <ref>PMID:30249808</ref>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
			[[Category: Mus musculus]]
	[[Category: Gilbert R]]		[[Category: Gilbert R]]
	[[Category: Ni T]]		[[Category: Ni T]]
	[[Category: Yu X]]		[[Category: Yu X]]
	[[Category: Zhang P]]		[[Category: Zhang P]]

OCA at 06:58, 20 July 2022

2022-07-20T06:58:53Z

← Older revision		Revision as of 06:58, 20 July 2022
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	~~'''Unreleased structure'''~~

	~~The entry~~ 8a1d is ~~ON HOLD until Paper Publication~~		==Structure of murine perforin-2 (Mpeg1) pore in ring form==
			<StructureSection load='8a1d' size='340' side='right'caption='[[8a1d]]' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1D FirstGlance]. <br>
	~~Description~~:		</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=8a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1d OCA], [https://pdbe.org/8a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1d RCSB], [https://www.ebi.ac.uk/pdbsum/8a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1d ProSAT]</span></td></tr>
	[[Category: ~~Unreleased Structures~~]]		</table>
			__TOC__
			</StructureSection>
			[[Category: Large Structures]]
			[[Category: Gilbert R]]
			[[Category: Ni T]]
			[[Category: Yu X]]
			[[Category: Zhang P]]

OCA at 04:05, 13 July 2022

2022-07-13T04:05:06Z

← Older revision		Revision as of 04:05, 13 July 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8a1d is ON HOLD		The entry 8a1d is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8a1d" [edit=sysop:move=sysop]

2022-06-08T04:22:59Z

Protected "8a1d" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:22, 8 June 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8a1d is ON HOLD Authors: Description: Category: Unreleased Structures

2022-06-08T04:22:58Z

New page: '''Unreleased structure''' The entry 8a1d is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8a1d is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]