4fyw - Revision history

OCA at 15:36, 14 March 2024

OCA — Thu, 14 Mar 2024 15:36:25 GMT

←Older revision		Revision as of 15:36, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</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]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [https://pdbe.org/4fyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [https://www.ebi.ac.uk/pdbsum/4fyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyw 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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [https://pdbe.org/4fyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [https://www.ebi.ac.uk/pdbsum/4fyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]		[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Escherichia coli aspartate transcarbamoylase (ATCase) allosterically regulates pyrimidine nucleotide biosynthesis. The enzyme is inhibited by CTP and can be further inhibited by UTP, although UTP alone has little or no influence on activity; however, the mechanism for the synergistic inhibition is still unknown. To determine how UTP is able to synergistically inhibit ATCase in the presence of CTP, we determined a series of X-ray structures of ATCase.nucleotide complexes. Analysis of the X-ray structures revealed that (1) CTP and dCTP bind in a very similar fashion, (2) UTP, in the presence of dCTP or CTP, binds at a site that does not overlap the CTP/dCTP site, and (3) the triphosphates of the two nucleotides are parallel to each other with a metal ion, in this case Mg(2+), coordinated between the beta- and gamma-phosphates of the two nucleotides. Kinetic experiments showed that the presence of a metal ion such as Mg(2+) is required for synergistic inhibition. Together, these results explain how the binding of UTP can enhance the binding of CTP and why UTP binds more tightly in the presence of CTP. A mechanism for the synergistic inhibition of ATCase is proposed in which the presence of UTP stabilizes the T state even more than CTP alone. These results also call into question many of the past kinetic and binding experiments with ATCase with nucleotides as the presence of metal contamination was not considered important.
-
-	Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase.,Cockrell GM, Kantrowitz ER Biochemistry. 2012 Sep 11;51(36):7128-37. Epub 2012 Aug 24. PMID:22906065<ref>PMID:22906065</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4fyw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Aspartate carbamoyltransferase 3D structures\|Aspartate carbamoyltransferase 3D structures]]		*[[Aspartate carbamoyltransferase 3D structures\|Aspartate carbamoyltransferase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:15, 19 October 2022

OCA — Wed, 19 Oct 2022 20:15:51 GMT

←Older revision		Revision as of 20:15, 19 October 2022
Line 3:		Line 3:
	<StructureSection load='4fyw' size='340' side='right'caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4fyw' size='340' side='right'caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Escherichia_coli~~ Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FYW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</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=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyv\|4fyv]], [[4fyx\|4fyx]], [[4fyy\|4fyy]]</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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [https://pdbe.org/4fyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [https://www.ebi.ac.uk/pdbsum/4fyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyw 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/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [~~http~~://pdbe.org/4fyw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fyw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyw ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~PYRI_ECOLI PYRI_ECOLI]] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002~~]	+	[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	~~[[Category: Aspartate carbamoyltransferase]]~~	+	[[Category: Escherichia coli K-12]]
-	[[Category: Escherichia coli]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cockrell~~, G M~~]]	+	[[Category: Cockrell GM]]
-	[[Category: Kantrowitz~~, E R]]~~	+	[[Category: Kantrowitz ER]]
-	~~[[Category: Allostery]]~~	+
-	~~[[Category: Feedback inhibition]]~~	+
-	~~[[Category: Pyrimidine nucleotide biosynthesis]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:27, 27 March 2019

OCA — Wed, 27 Mar 2019 08:27:07 GMT

←Older revision		Revision as of 08:27, 27 March 2019
Line 1:		Line 1:

	==E. coli Aspartate Transcarbamoylase complexed with CTP==		==E. coli Aspartate Transcarbamoylase complexed with CTP==
-	<StructureSection load='4fyw' size='340' side='right' caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4fyw' size='340' side='right'caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYW FirstGlance]. <br>
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Aspartate carbamoyltransferase\|Aspartate carbamoyltransferase]]	+	*[[Aspartate carbamoyltransferase 3D structures\|Aspartate carbamoyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	[[Category: Aspartate carbamoyltransferase]]		[[Category: Aspartate carbamoyltransferase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
		+	[[Category: Large Structures]]
	[[Category: Cockrell, G M]]		[[Category: Cockrell, G M]]
	[[Category: Kantrowitz, E R]]		[[Category: Kantrowitz, E R]]

OCA at 10:29, 5 August 2016

OCA — Fri, 05 Aug 2016 10:29:03 GMT

←Older revision		Revision as of 10:29, 5 August 2016
Line 1:		Line 1:
		+
	==E. coli Aspartate Transcarbamoylase complexed with CTP==		==E. coli Aspartate Transcarbamoylase complexed with CTP==
	<StructureSection load='4fyw' size='340' side='right' caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4fyw' size='340' side='right' caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyv\|4fyv]], [[4fyx\|4fyx]], [[4fyy\|4fyy]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyv\|4fyv]], [[4fyx\|4fyx]], [[4fyy\|4fyy]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [http://www.ebi.ac.uk/pdbsum/4fyw 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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [http://pdbe.org/4fyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [http://www.ebi.ac.uk/pdbsum/4fyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyw 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 4fyw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 18:02, 25 December 2014

OCA — Thu, 25 Dec 2014 18:02:41 GMT

←Older revision		Revision as of 18:02, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyv\|4fyv]], [[4fyx\|4fyx]], [[4fyy\|4fyy]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyv\|4fyv]], [[4fyx\|4fyx]], [[4fyy\|4fyy]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [http://www.ebi.ac.uk/pdbsum/4fyw 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=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [http://www.ebi.ac.uk/pdbsum/4fyw PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PYRI_ECOLI PYRI_ECOLI]] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 27:
	[[Category: Aspartate carbamoyltransferase]]		[[Category: Aspartate carbamoyltransferase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Cockrell, G M.]]	+	[[Category: Cockrell, G M]]
-	[[Category: Kantrowitz, E R.]]	+	[[Category: Kantrowitz, E R]]
	[[Category: Allostery]]		[[Category: Allostery]]
	[[Category: Feedback inhibition]]		[[Category: Feedback inhibition]]
	[[Category: Pyrimidine nucleotide biosynthesis]]		[[Category: Pyrimidine nucleotide biosynthesis]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 10:45, 16 July 2014

OCA — Wed, 16 Jul 2014 10:45:27 GMT

←Older revision		Revision as of 10:45, 16 July 2014
Line 1:		Line 1:
-	[[~~Image:~~4fyw.~~jpg~~\|~~left~~\|~~200px~~]]	+	==E. coli Aspartate Transcarbamoylase complexed with CTP==
		+	<StructureSection load='4fyw' size='340' side='right' caption='[[4fyw]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4fyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyv\|4fyv]], [[4fyx\|4fyx]], [[4fyy\|4fyy]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyw RCSB], [http://www.ebi.ac.uk/pdbsum/4fyw PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Escherichia coli aspartate transcarbamoylase (ATCase) allosterically regulates pyrimidine nucleotide biosynthesis. The enzyme is inhibited by CTP and can be further inhibited by UTP, although UTP alone has little or no influence on activity; however, the mechanism for the synergistic inhibition is still unknown. To determine how UTP is able to synergistically inhibit ATCase in the presence of CTP, we determined a series of X-ray structures of ATCase.nucleotide complexes. Analysis of the X-ray structures revealed that (1) CTP and dCTP bind in a very similar fashion, (2) UTP, in the presence of dCTP or CTP, binds at a site that does not overlap the CTP/dCTP site, and (3) the triphosphates of the two nucleotides are parallel to each other with a metal ion, in this case Mg(2+), coordinated between the beta- and gamma-phosphates of the two nucleotides. Kinetic experiments showed that the presence of a metal ion such as Mg(2+) is required for synergistic inhibition. Together, these results explain how the binding of UTP can enhance the binding of CTP and why UTP binds more tightly in the presence of CTP. A mechanism for the synergistic inhibition of ATCase is proposed in which the presence of UTP stabilizes the T state even more than CTP alone. These results also call into question many of the past kinetic and binding experiments with ATCase with nucleotides as the presence of metal contamination was not considered important.

-	~~{{STRUCTURE_4fyw\| PDB=4fyw \| SCENE= }}~~	+	Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase.,Cockrell GM, Kantrowitz ER Biochemistry. 2012 Sep 11;51(36):7128-37. Epub 2012 Aug 24. PMID:22906065<ref>PMID:22906065</ref>

-	~~===E~~. ~~coli Aspartate Transcarbamoylase complexed with CTP===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_22906065}}~~	+	==See Also==
-		+	*[[Aspartate carbamoyltransferase\|Aspartate carbamoyltransferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4fyw~~]] ~~is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Aspartate carbamoyltransferase]]		[[Category: Aspartate carbamoyltransferase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]

OCA at 07:21, 10 October 2012

OCA — Wed, 10 Oct 2012 07:21:39 GMT

←Older revision		Revision as of 07:21, 10 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4fyw.jpg\|left\|200px]]

-	~~The entry~~ 4fyw ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4fyw\| PDB=4fyw \| SCENE= }}

-	~~Authors: Cockrell, G.M., Kantrowitz,~~ E.R.	+	===E. coli Aspartate Transcarbamoylase complexed with CTP===

-	~~Description~~: E. coli Aspartate ~~Transcarbamoylase complexed with CTP~~	+	{{ABSTRACT_PUBMED_22906065}}
		+
		+	==About this Structure==
		+	[[4fyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYW OCA].
		+	[[Category: Aspartate carbamoyltransferase]]
		+	[[Category: Escherichia coli]]
		+	[[Category: Cockrell, G M.]]
		+	[[Category: Kantrowitz, E R.]]
		+	[[Category: Allostery]]
		+	[[Category: Feedback inhibition]]
		+	[[Category: Pyrimidine nucleotide biosynthesis]]
		+	[[Category: Transferase]]

OCA at 06:49, 25 July 2012

OCA — Wed, 25 Jul 2012 06:49:28 GMT

←Older revision		Revision as of 06:49, 25 July 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Cockrell, G.M., Kantrowitz, E.R.		Authors: Cockrell, G.M., Kantrowitz, E.R.

	Description: E. coli Aspartate Transcarbamoylase complexed with CTP		Description: E. coli Aspartate Transcarbamoylase complexed with CTP

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

OCA — Wed, 11 Jul 2012 07:54:07 GMT

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

←Older revision

Revision as of 07:54, 11 July 2012

OCA: New page: '''Unreleased structure''' The entry 4fyw is ON HOLD Authors: Cockrell, G.M., Kantrowitz, E.R. Description: E. coli Aspartate Transcarbamoylase complexed with CTP

OCA — Wed, 11 Jul 2012 07:54:06 GMT

New page: '''Unreleased structure''' The entry 4fyw is ON HOLD Authors: Cockrell, G.M., Kantrowitz, E.R. Description: E. coli Aspartate Transcarbamoylase complexed with CTP

New page

'''Unreleased structure'''

The entry 4fyw is ON HOLD

Authors: Cockrell, G.M., Kantrowitz, E.R.

Description: E. coli Aspartate Transcarbamoylase complexed with CTP