4c6b - Revision history

OCA at 12:04, 20 December 2023

2023-12-20T12:04:43Z

←Older revision		Revision as of 12:04, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6B FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6B FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.656Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [https://pdbe.org/4c6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [https://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b 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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [https://pdbe.org/4c6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [https://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b 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 4c6b" 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 17:28, 7 September 2022

2022-09-07T17:28:56Z

←Older revision		Revision as of 17:28, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c6b' size='340' side='right'caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>		<StructureSection load='4c6b' size='340' side='right'caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C6B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6B FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6i\|4c6i]], [[4c6j\|4c6j]], [[4c6k\|4c6k]], [[4c6l\|4c6l]], [[4c6m\|4c6m]], [[4c6n\|4c6n]], [[4c6o\|4c6o]], [[4c6p\|4c6p]], [[4c6q\|4c6q]]</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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [https://pdbe.org/4c6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [https://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b 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/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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [~~http~~://pdbe.org/4c6b PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b 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 4c6b" 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 08:51, 20 March 2019

2019-03-20T08:51:16Z

←Older revision		Revision as of 08:51, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==		==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==
-	<StructureSection load='4c6b' size='340' side='right' caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>	+	<StructureSection load='4c6b' size='340' side='right'caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6B FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6B FirstGlance]. <br>
Line 26:		Line 26:
	[[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 15:47, 5 August 2016

2016-08-05T15:47:14Z

←Older revision		Revision as of 15:47, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==		==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==
	<StructureSection load='4c6b' size='340' side='right' caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>		<StructureSection load='4c6b' size='340' side='right' caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6i\|4c6i]], [[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">[[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6i\|4c6i]], [[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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [http://www.ebi.ac.uk/pdbsum/4c6b 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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [http://pdbe.org/4c6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [http://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4c6b" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:43, 25 December 2014

2014-12-25T03:43:10Z

←Older revision		Revision as of 03:43, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c6b\| PDB=4c6b \| SCENE= }}~~	+	==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==
-	===Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.===	+	<StructureSection load='4c6b' size='340' side='right' caption='[[4c6b]], [[Resolution\|resolution]] 1.66Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24332717}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6B FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c6c\|4c6c]], [[4c6d\|4c6d]], [[4c6e\|4c6e]], [[4c6f\|4c6f]], [[4c6i\|4c6i]], [[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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [http://www.ebi.ac.uk/pdbsum/4c6b 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>
-	~~[[4c6b]] is a 1 chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=4C6B 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 11:08, 5 February 2014

2014-02-05T11:08:04Z

←Older revision		Revision as of 11:08, 5 February 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4c6b\| PDB=4c6b \| SCENE= }}
		+	===Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.===
		+	{{ABSTRACT_PUBMED_24332717}}

-	~~The entry 4c6b~~ 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==
		+	[[4c6b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6B OCA].

-	~~Description~~: ~~Crystal structure of the dihydroorotase domain of human CAD with incomplete active site~~, ~~obtained recombinantly from E~~. ~~coli~~.	+	==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: Protected "4c6b" [edit=sysop:move=sysop]

2013-09-29T07:15:55Z

Protected "4c6b" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:15, 29 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c6b is ON HOLD until Paper Publication Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A. Description: Crystal structure of the dihydrooro...

2013-09-29T07:15:54Z

New page: '''Unreleased structure''' The entry 4c6b is ON HOLD until Paper Publication Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A. Description: Crystal structure of the dihydrooro...

New page

'''Unreleased structure'''

The entry 4c6b is ON HOLD until Paper Publication

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

Description: Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.