8afg - Revision history

OCA at 07:56, 1 May 2024

OCA — Wed, 01 May 2024 07:56:34 GMT

←Older revision		Revision as of 07:56, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8afg]] is a 2 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=8AFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFG FirstGlance]. <br>		<table><tr><td colspan='2'>[[8afg]] is a 2 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=8AFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.45Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afg OCA], [https://pdbe.org/8afg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afg RCSB], [https://www.ebi.ac.uk/pdbsum/8afg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afg 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=8afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afg OCA], [https://pdbe.org/8afg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afg RCSB], [https://www.ebi.ac.uk/pdbsum/8afg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/FAT2_YEAST FAT2_YEAST] Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.<ref>PMID:24291261</ref>		[https://www.uniprot.org/uniprot/FAT2_YEAST FAT2_YEAST] Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.<ref>PMID:24291261</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Oxalyl-CoA synthetase from Saccharomyces cerevisiae is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting Signal 1, which however is partly dispensable, suggesting additional receptor bindings sites. To unravel any additional features that may contribute to its capacity to be recognized as peroxisomal target, we determined its assembly and overall architecture by an integrated structural biology approach, including X-ray crystallography, single particle cryo-electron microscopy and small angle X-ray scattering. Surprisingly, it assembles into mixture of concentration-dependent dimers, tetramers and hexamers by dimer self-association. Hexameric particles form an unprecedented asymmetric horseshoe-like arrangement, which considerably differs from symmetric hexameric assembly found in many other protein structures. A single mutation within the self-association interface is sufficient to abolish any higher-level oligomerization, resulting in a homogenous dimeric assembly. The small C-terminal domain of yeast Oxalyl-CoA synthetase is connected by a partly flexible hinge with the large N-terminal domain, which provides the sole basis for oligomeric assembly. Our data provide a basis to mechanistically study peroxisomal translocation of this target.
-
-	Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase.,Burgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M Biol Chem. 2023 Jan 26. doi: 10.1515/hsz-2022-0273. PMID:36694962<ref>PMID:36694962</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8afg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:45, 8 February 2023

OCA — Wed, 08 Feb 2023 06:45:25 GMT

←Older revision		Revision as of 06:45, 8 February 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8afg is ~~ON HOLD until Paper~~ Publication	+	==K352D oxalyl-CoA synthetase Pcs60p==
		+	<StructureSection load='8afg' size='340' side='right'caption='[[8afg]], [[Resolution\|resolution]] 2.45Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8afg]] is a 2 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=8AFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afg OCA], [https://pdbe.org/8afg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afg RCSB], [https://www.ebi.ac.uk/pdbsum/8afg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afg ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/FAT2_YEAST FAT2_YEAST] Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.<ref>PMID:24291261</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Oxalyl-CoA synthetase from Saccharomyces cerevisiae is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting Signal 1, which however is partly dispensable, suggesting additional receptor bindings sites. To unravel any additional features that may contribute to its capacity to be recognized as peroxisomal target, we determined its assembly and overall architecture by an integrated structural biology approach, including X-ray crystallography, single particle cryo-electron microscopy and small angle X-ray scattering. Surprisingly, it assembles into mixture of concentration-dependent dimers, tetramers and hexamers by dimer self-association. Hexameric particles form an unprecedented asymmetric horseshoe-like arrangement, which considerably differs from symmetric hexameric assembly found in many other protein structures. A single mutation within the self-association interface is sufficient to abolish any higher-level oligomerization, resulting in a homogenous dimeric assembly. The small C-terminal domain of yeast Oxalyl-CoA synthetase is connected by a partly flexible hinge with the large N-terminal domain, which provides the sole basis for oligomeric assembly. Our data provide a basis to mechanistically study peroxisomal translocation of this target.

-	~~Authors: Burgi~~, J., ~~Chojnowski~~, G., ~~Wilmanns~~, M.	+	Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase.,Burgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M Biol Chem. 2023 Jan 26. doi: 10.1515/hsz-2022-0273. PMID:36694962<ref>PMID:36694962</ref>

-	~~Description: K352D oxalyl~~-~~CoA synthetase Pcs60p~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: ~~Wilmanns, M~~]]	+	<div class="pdbe-citations 8afg" style="background-color:#fffaf0;"></div>
-	[[Category: Chojnowski, G]]	+	== References ==
-	[[Category: ~~Burgi, J~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Saccharomyces cerevisiae]]
		+	[[Category: Burgi J]]
		+	[[Category: Chojnowski G]]
		+	[[Category: Wilmanns M]]

OCA at 05:34, 14 September 2022

OCA — Wed, 14 Sep 2022 05:34:11 GMT

←Older revision		Revision as of 05:34, 14 September 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8afg is ON HOLD	+	The entry 8afg is ON HOLD until Paper Publication

	Authors: Burgi, J., Chojnowski, G., Wilmanns, M.		Authors: Burgi, J., Chojnowski, G., Wilmanns, M.

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

OCA — Wed, 27 Jul 2022 16:34:25 GMT

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

←Older revision

Revision as of 16:34, 27 July 2022

OCA: New page: '''Unreleased structure''' The entry 8afg is ON HOLD Authors: Burgi, J., Chojnowski, G., Wilmanns, M. Description: K352D oxalyl-CoA synthetase Pcs60p [[Category: Unreleased Structures]...

OCA — Wed, 27 Jul 2022 16:34:23 GMT

New page: '''Unreleased structure''' The entry 8afg is ON HOLD Authors: Burgi, J., Chojnowski, G., Wilmanns, M. Description: K352D oxalyl-CoA synthetase Pcs60p [[Category: Unreleased Structures]...

New page

'''Unreleased structure'''

The entry 8afg is ON HOLD

Authors: Burgi, J., Chojnowski, G., Wilmanns, M.

Description: K352D oxalyl-CoA synthetase Pcs60p
[[Category: Unreleased Structures]]
[[Category: Wilmanns, M]]
[[Category: Chojnowski, G]]
[[Category: Burgi, J]]