5uqu - Revision history

OCA at 14:28, 6 March 2024

OCA — Wed, 06 Mar 2024 14:28:47 GMT

←Older revision		Revision as of 14:28, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='5uqu' size='340' side='right'caption='[[5uqu]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='5uqu' size='340' side='right'caption='[[5uqu]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5uqu]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Aspfm Aspfm~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5UQU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5uqu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UQU FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=COA:COENZYME+A'>COA</scene>~~, ~~<scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <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]] 1.7Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5uqo\|5uqo]], [[5uqq\|5uqq]], [[5uqr\|5uqr]], [[5uqs\|5uqs]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<~~tr id~~='~~gene~~'><~~td class="sblockLbl"~~><~~b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">mcsA, cit1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])~~</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=5uqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqu OCA], [https://pdbe.org/5uqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uqu RCSB], [https://www.ebi.ac.uk/pdbsum/5uqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqu 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=5uqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqu OCA], [~~http~~://pdbe.org/5uqu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5uqu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5uqu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqu ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PRPC_ASPFM PRPC_ASPFM]] Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA and oxaloacetate. May play a role in virulence.<ref>PMID:16008561</ref>	+	[https://www.uniprot.org/uniprot/PRPC_ASPFM PRPC_ASPFM] Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA and oxaloacetate. May play a role in virulence.<ref>PMID:16008561</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Aspergillus fumigatus is a ubiquitous fungus that is not only a problem in agriculture, but also in healthcare. Aspergillus fumigatus drug resistance is becoming more prominent which is mainly attributed to the widespread use of fungicides in agriculture. The fungi-specific 2-methylcitrate cycle is responsible for detoxifying propionyl-CoA, a toxic metabolite produced as the fungus breaks down proteins and amino acids. The enzyme responsible for this detoxification is 2-methylcitrate synthase (mcsA) and is a potential candidate for the design of new anti-fungals. However, mcsA is very similar in structure to human citrate synthase (hCS) and catalyzes the same reaction. Therefore, both enzymes were studied in parallel to provide foundations for design of mcsA-specific inhibitors. The first crystal structures of citrate synthase from humans and 2-methylcitrate synthase from A. fumigatus are reported. The determined structures capture various conformational states of the enzymes and several inhibitors were identified and characterized. Despite a significant homology, mcsA and hCS display pronounced differences in substrate specificity and cooperativity. Considering that the active sites of the enzymes are almost identical, the differences in reactions catalyzed by enzymes are caused by residues that are in the vicinity of the active site and influence conformational changes of the enzymes.	+
-		+
-	Comparative studies of Aspergillus fumigatus 2-methylcitrate synthase and human citrate synthase.,Schlachter CR, Klapper V, Radford T, Chruszcz M Biol Chem. 2019 Nov 26;400(12):1567-1581. doi: 10.1515/hsz-2019-0106. PMID:31141475<ref>PMID:31141475</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5uqu" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 28:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aspfm~~]]	+	[[Category: Aspergillus fumigatus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chruszcz, M]]	+	[[Category: Chruszcz M]]
-	[[Category: Schlachter, C]]	+	[[Category: Schlachter C]]
-	~~[[Category: 2-methylcitrate synthase]]~~	+
-	~~[[Category: Aspergillus fumigatus]]~~	+
-	~~[[Category: Citrate synthase]]~~	+
-	~~[[Category: Mcsa]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:30, 17 June 2020

OCA — Wed, 17 Jun 2020 10:30:16 GMT

←Older revision		Revision as of 10:30, 17 June 2020
Line 1:		Line 1:

	==Crystal structure of mutant 2-methylcitrate synthase (mcsAG352A) from Aspergillus fumigatus==		==Crystal structure of mutant 2-methylcitrate synthase (mcsAG352A) from Aspergillus fumigatus==
-	<StructureSection load='5uqu' size='340' side='right' caption='[[5uqu]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='5uqu' size='340' side='right'caption='[[5uqu]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5uqu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQU OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5UQU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5uqu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UQU FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5uqo\|5uqo]], [[5uqq\|5uqq]], [[5uqr\|5uqr]], [[5uqs\|5uqs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5uqo\|5uqo]], [[5uqq\|5uqq]], [[5uqr\|5uqr]], [[5uqs\|5uqs]]</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=5uqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqu OCA], [http://pdbe.org/5uqu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uqu RCSB], [http://www.ebi.ac.uk/pdbsum/5uqu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqu ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mcsA, cit1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</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=5uqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqu OCA], [http://pdbe.org/5uqu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uqu RCSB], [http://www.ebi.ac.uk/pdbsum/5uqu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PRPC_ASPFM PRPC_ASPFM]] Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA and oxaloacetate. May play a role in virulence.<ref>PMID:16008561</ref>		[[http://www.uniprot.org/uniprot/PRPC_ASPFM PRPC_ASPFM]] Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA and oxaloacetate. May play a role in virulence.<ref>PMID:16008561</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Aspergillus fumigatus is a ubiquitous fungus that is not only a problem in agriculture, but also in healthcare. Aspergillus fumigatus drug resistance is becoming more prominent which is mainly attributed to the widespread use of fungicides in agriculture. The fungi-specific 2-methylcitrate cycle is responsible for detoxifying propionyl-CoA, a toxic metabolite produced as the fungus breaks down proteins and amino acids. The enzyme responsible for this detoxification is 2-methylcitrate synthase (mcsA) and is a potential candidate for the design of new anti-fungals. However, mcsA is very similar in structure to human citrate synthase (hCS) and catalyzes the same reaction. Therefore, both enzymes were studied in parallel to provide foundations for design of mcsA-specific inhibitors. The first crystal structures of citrate synthase from humans and 2-methylcitrate synthase from A. fumigatus are reported. The determined structures capture various conformational states of the enzymes and several inhibitors were identified and characterized. Despite a significant homology, mcsA and hCS display pronounced differences in substrate specificity and cooperativity. Considering that the active sites of the enzymes are almost identical, the differences in reactions catalyzed by enzymes are caused by residues that are in the vicinity of the active site and influence conformational changes of the enzymes.
		+
		+	Comparative studies of Aspergillus fumigatus 2-methylcitrate synthase and human citrate synthase.,Schlachter CR, Klapper V, Radford T, Chruszcz M Biol Chem. 2019 Nov 26;400(12):1567-1581. doi: 10.1515/hsz-2019-0106. PMID:31141475<ref>PMID:31141475</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5uqu" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Citrate Synthase 3D structures\|Citrate Synthase 3D structures]]
		+	*[[Methylcitrate synthase\|Methylcitrate synthase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aspfm]]
		+	[[Category: Large Structures]]
	[[Category: Chruszcz, M]]		[[Category: Chruszcz, M]]
	[[Category: Schlachter, C]]		[[Category: Schlachter, C]]

OCA at 06:27, 15 February 2018

OCA — Thu, 15 Feb 2018 06:27:43 GMT

←Older revision		Revision as of 06:27, 15 February 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 5uqu is ON HOLD until Paper Publication~~	+	==Crystal structure of mutant 2-methylcitrate synthase (mcsAG352A) from Aspergillus fumigatus==
-		+	<StructureSection load='5uqu' size='340' side='right' caption='[[5uqu]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~Authors: Schlachter, C., Chruszcz, M.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5uqu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UQU FirstGlance]. <br>
-	~~Description:~~ Crystal structure of mutant 2-methylcitrate synthase (mcsAG352A) from Aspergillus fumigatus	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5uqo\|5uqo]], [[5uqq\|5uqq]], [[5uqr\|5uqr]], [[5uqs\|5uqs]]</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=5uqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqu OCA], [http://pdbe.org/5uqu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uqu RCSB], [http://www.ebi.ac.uk/pdbsum/5uqu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqu ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PRPC_ASPFM PRPC_ASPFM]] Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA and oxaloacetate. May play a role in virulence.<ref>PMID:16008561</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Chruszcz, M]]		[[Category: Chruszcz, M]]
	[[Category: Schlachter, C]]		[[Category: Schlachter, C]]
		+	[[Category: 2-methylcitrate synthase]]
		+	[[Category: Aspergillus fumigatus]]
		+	[[Category: Citrate synthase]]
		+	[[Category: Mcsa]]
		+	[[Category: Transferase]]

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

OCA — Thu, 09 Mar 2017 14:48:13 GMT

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

←Older revision

Revision as of 14:48, 9 March 2017

OCA: New page: '''Unreleased structure''' The entry 5uqu is ON HOLD until Paper Publication Authors: Schlachter, C., Chruszcz, M. Description: Crystal structure of mutant 2-methylcitrate synthase (mc...

OCA — Thu, 09 Mar 2017 14:48:11 GMT

New page: '''Unreleased structure''' The entry 5uqu is ON HOLD until Paper Publication Authors: Schlachter, C., Chruszcz, M. Description: Crystal structure of mutant 2-methylcitrate synthase (mc...

New page

'''Unreleased structure'''

The entry 5uqu is ON HOLD until Paper Publication

Authors: Schlachter, C., Chruszcz, M.

Description: Crystal structure of mutant 2-methylcitrate synthase (mcsAG352A) from Aspergillus fumigatus
[[Category: Unreleased Structures]]
[[Category: Chruszcz, M]]
[[Category: Schlachter, C]]