4c6i - Revision history

OCA at 12:04, 20 December 2023

OCA — Wed, 20 Dec 2023 12:04:51 GMT

←Older revision		Revision as of 12:04, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6I FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6I FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.35Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [https://pdbe.org/4c6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [https://www.ebi.ac.uk/pdbsum/4c6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6i 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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [https://pdbe.org/4c6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [https://www.ebi.ac.uk/pdbsum/4c6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).	+	[https://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Upregulation of CAD, the multifunctional protein that initiates and controls the de novo biosynthesis of pyrimidines in animals, is essential for cell proliferation. Deciphering the architecture and functioning of CAD is of interest for its potential usage as an antitumoral target. However, there is no detailed structural information about CAD other than that it self-assembles into hexamers of approximately 1.5 MDa. Here we report the crystal structure and functional characterization of the dihydroorotase domain of human CAD. Contradicting all assumptions, the structure reveals an active site enclosed by a flexible loop with two Zn2+ ions bridged by a carboxylated lysine and a third Zn coordinating a rare histidinate ion. Site-directed mutagenesis and functional assays prove the involvement of the Zn and flexible loop in catalysis. Comparison with homologous bacterial enzymes supports a reclassification of the DHOase family and provides strong evidence against current models of the architecture of CAD.
		+
		+	Structure, Functional Characterization, and Evolution of the Dihydroorotase Domain of Human CAD.,Grande-Garcia A, Lallous N, Diaz-Tejada C, Ramon-Maiques S Structure. 2013 Dec 10. pii: S0969-2126(13)00428-0. doi:, 10.1016/j.str.2013.10.016. PMID:24332717<ref>PMID:24332717</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c6i" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[CAD protein 3D structures\|CAD protein 3D structures]]		*[[CAD protein 3D structures\|CAD protein 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:29, 7 September 2022

OCA — Wed, 07 Sep 2022 17:29:10 GMT

←Older revision		Revision as of 17:29, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c6i' size='340' side='right'caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>		<StructureSection load='4c6i' size='340' side='right'caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C6I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6I FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=~~NCD~~:N-~~CARBAMOYL-L-ASPARTATE~~'>~~NCD~~</scene>, <scene name='pdbligand=ZN:~~ZINC+ION~~'>ZN</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~KCX~~:~~LYSINE~~+~~NZ-CARBOXYLIC+ACID~~'>~~KCX~~</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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [https://pdbe.org/4c6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [https://www.ebi.ac.uk/pdbsum/4c6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6i ProSAT]</span></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6b\|4c6b]], [[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6j\|4c6j]], [[4c6k\|4c6k]], [[4c6l\|4c6l]], [[4c6m\|4c6m]], [[4c6n\|4c6n]], [[4c6o\|4c6o]], [[4c6p\|4c6p]], [[4c6q\|4c6q]]</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] </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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [~~http~~://pdbe.org/4c6i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c6i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6i ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).	+	[[https://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Upregulation of CAD, the multifunctional protein that initiates and controls the de novo biosynthesis of pyrimidines in animals, is essential for cell proliferation. Deciphering the architecture and functioning of CAD is of interest for its potential usage as an antitumoral target. However, there is no detailed structural information about CAD other than that it self-assembles into hexamers of approximately 1.5 MDa. Here we report the crystal structure and functional characterization of the dihydroorotase domain of human CAD. Contradicting all assumptions, the structure reveals an active site enclosed by a flexible loop with two Zn2+ ions bridged by a carboxylated lysine and a third Zn coordinating a rare histidinate ion. Site-directed mutagenesis and functional assays prove the involvement of the Zn and flexible loop in catalysis. Comparison with homologous bacterial enzymes supports a reclassification of the DHOase family and provides strong evidence against current models of the architecture of CAD.	+

-	Structure, Functional Characterization, and Evolution of the Dihydroorotase Domain of Human CAD.,Grande-Garcia A, Lallous N, Diaz-Tejada C, Ramon-Maiques S Structure. 2013 Dec 10. pii: S0969-2126(13)00428-0. doi:, 10.1016/j.str.2013.10.016. PMID:24332717<ref>PMID:24332717</ref>	+	==See Also==
-		+	*[[CAD protein 3D structures\|CAD protein 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 4c6i" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Dihydroorotase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Grande-Garcia, A]]	+	[[Category: Grande-Garcia A]]
-	[[Category: Lallous, N]]	+	[[Category: Lallous N]]
-	[[Category: Ramon-Maiques, S]]	+	[[Category: Ramon-Maiques S]]
-	~~[[Category: Amidohydrolase superfamily]]~~	+
-	~~[[Category: De novo pyrimidine biosynthesis]]~~	+
-	~~[[Category: Histidinate anion]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metalloenzyme]]~~	+
-	~~[[Category: Zinc binding~~]]	+

OCA at 09:36, 20 March 2019

OCA — Wed, 20 Mar 2019 09:36:52 GMT

←Older revision		Revision as of 09:36, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0==		==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0==
-	<StructureSection load='4c6i' size='340' side='right' caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>	+	<StructureSection load='4c6i' size='340' side='right'caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6I FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6I FirstGlance]. <br>
Line 27:		Line 27:
	[[Category: Dihydroorotase]]		[[Category: Dihydroorotase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Grande-Garcia, A]]		[[Category: Grande-Garcia, A]]
	[[Category: Lallous, N]]		[[Category: Lallous, N]]

OCA at 22:08, 4 August 2016

OCA — Thu, 04 Aug 2016 22:08:24 GMT

←Older revision		Revision as of 22:08, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0==		==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0==
	<StructureSection load='4c6i' size='340' side='right' caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>		<StructureSection load='4c6i' size='340' side='right' caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6b\|4c6b]], [[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6j\|4c6j]], [[4c6k\|4c6k]], [[4c6l\|4c6l]], [[4c6m\|4c6m]], [[4c6n\|4c6n]], [[4c6o\|4c6o]], [[4c6p\|4c6p]], [[4c6q\|4c6q]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6b\|4c6b]], [[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6j\|4c6j]], [[4c6k\|4c6k]], [[4c6l\|4c6l]], [[4c6m\|4c6m]], [[4c6n\|4c6n]], [[4c6o\|4c6o]], [[4c6p\|4c6p]], [[4c6q\|4c6q]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] </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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [http://www.ebi.ac.uk/pdbsum/4c6i PDBsum]</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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [http://pdbe.org/4c6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [http://www.ebi.ac.uk/pdbsum/4c6i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4c6i" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:32, 25 December 2014

OCA — Thu, 25 Dec 2014 13:32:55 GMT

←Older revision		Revision as of 13:32, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c6i\| PDB=4c6i \| SCENE= }}~~	+	==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0==
-	===Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0===	+	<StructureSection load='4c6i' size='340' side='right' caption='[[4c6i]], [[Resolution\|resolution]] 1.35Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24332717}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c6i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6I FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6b\|4c6b]], [[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6j\|4c6j]], [[4c6k\|4c6k]], [[4c6l\|4c6l]], [[4c6m\|4c6m]], [[4c6n\|4c6n]], [[4c6o\|4c6o]], [[4c6p\|4c6p]], [[4c6q\|4c6q]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] </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=4c6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c6i RCSB], [http://www.ebi.ac.uk/pdbsum/4c6i PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).		[[http://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Upregulation of CAD, the multifunctional protein that initiates and controls the de novo biosynthesis of pyrimidines in animals, is essential for cell proliferation. Deciphering the architecture and functioning of CAD is of interest for its potential usage as an antitumoral target. However, there is no detailed structural information about CAD other than that it self-assembles into hexamers of approximately 1.5 MDa. Here we report the crystal structure and functional characterization of the dihydroorotase domain of human CAD. Contradicting all assumptions, the structure reveals an active site enclosed by a flexible loop with two Zn2+ ions bridged by a carboxylated lysine and a third Zn coordinating a rare histidinate ion. Site-directed mutagenesis and functional assays prove the involvement of the Zn and flexible loop in catalysis. Comparison with homologous bacterial enzymes supports a reclassification of the DHOase family and provides strong evidence against current models of the architecture of CAD.

-	~~==About this~~ Structure==	+	Structure, Functional Characterization, and Evolution of the Dihydroorotase Domain of Human CAD.,Grande-Garcia A, Lallous N, Diaz-Tejada C, Ramon-Maiques S Structure. 2013 Dec 10. pii: S0969-2126(13)00428-0. doi:, 10.1016/j.str.2013.10.016. PMID:24332717<ref>PMID:24332717</ref>
-	~~[[4c6i]] is a 1 chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=4C6I OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024332717</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Dihydroorotase]]		[[Category: Dihydroorotase]]
-	[[Category: Grande-Garcia, A.]]	+	[[Category: Human]]
-	[[Category: Lallous, N.]]	+	[[Category: Grande-Garcia, A]]
-	[[Category: Ramon-Maiques, S.]]	+	[[Category: Lallous, N]]
		+	[[Category: Ramon-Maiques, S]]
	[[Category: Amidohydrolase superfamily]]		[[Category: Amidohydrolase superfamily]]
	[[Category: De novo pyrimidine biosynthesis]]		[[Category: De novo pyrimidine biosynthesis]]

OCA at 10:32, 8 January 2014

OCA — Wed, 08 Jan 2014 10:32:17 GMT

←Older revision		Revision as of 10:32, 8 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4c6i\| PDB=4c6i \| SCENE= }}
		+	===Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0===
		+	{{ABSTRACT_PUBMED_24332717}}

-	~~The entry 4c6i~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

-	~~Authors~~: ~~Ramon-Maiques, S~~.~~, Lallous, N~~.~~, Grande~~-~~Garcia, A~~.	+	==About this Structure==
		+	[[4c6i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6I OCA].

-	~~Description~~: ~~Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7~~.0	+	==Reference==
		+	<ref group="xtra">PMID:024332717</ref><references group="xtra"/><references/>
		+	[[Category: Dihydroorotase]]
		+	[[Category: Grande-Garcia, A.]]
		+	[[Category: Lallous, N.]]
		+	[[Category: Ramon-Maiques, S.]]
		+	[[Category: Amidohydrolase superfamily]]
		+	[[Category: De novo pyrimidine biosynthesis]]
		+	[[Category: Histidinate anion]]
		+	[[Category: Hydrolase]]
		+	[[Category: Metalloenzyme]]
		+	[[Category: Zinc binding]]

OCA at 06:32, 2 October 2013

OCA — Wed, 02 Oct 2013 06:32:34 GMT

←Older revision		Revision as of 06:32, 2 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c6i is ON HOLD	+	The entry 4c6i is ON HOLD until Paper Publication

	Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A.		Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A.

	Description: Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0		Description: Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0

OCA: Protected "4c6i" [edit=sysop:move=sysop]

OCA — Sun, 29 Sep 2013 07:16:10 GMT

Protected "4c6i" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:16, 29 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c6i is ON HOLD Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A. Description: Crystal structure of the dihydroorotase domain of human CAD...

OCA — Sun, 29 Sep 2013 07:16:09 GMT

New page: '''Unreleased structure''' The entry 4c6i is ON HOLD Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A. Description: Crystal structure of the dihydroorotase domain of human CAD...

New page

'''Unreleased structure'''

The entry 4c6i is ON HOLD

Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A.

Description: Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0