4xds - Revision history

OCA at 13:00, 1 March 2024

OCA — Fri, 01 Mar 2024 13:00:35 GMT

←Older revision		Revision as of 13:00, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4xds]] is a 6 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=4XDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XDS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4xds]] is a 6 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=4XDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XDS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 3.354Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [https://pdbe.org/4xds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [https://www.ebi.ac.uk/pdbsum/4xds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds 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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [https://pdbe.org/4xds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [https://www.ebi.ac.uk/pdbsum/4xds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>		[https://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The E. coli dgt gene encodes a dGTP triphosphohydrolase whose detailed role still remains to be determined. Deletion of dgt creates a mutator phenotype, indicating that the dGTPase has a fidelity role, possibly by affecting the cellular dNTP pool. In the present study, we have investigated the structure of Dgt protein at 3.1 A resolution. One of the obtained structures revealed a protein hexamer that contained two molecules of single-stranded DNA. The presence of DNA caused significant conformational changes in the enzyme, including in the enzyme's catalytic site. Dgt preparations lacking DNA were able to bind ssDNA with high affinity (Kd ~ 50 nM). DNA binding positively affected the enzyme's activity: dGTPase activity displayed sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP. A mutant Dgt enzyme was also created containing residue changes in the DNA binding cleft. This mutant enzyme, while still active, was incapable of DNA binding and could no longer be stimulated by addition of DNA. We also created an E. coli strain containing the mutant dgt gene on the chromosome replacing the wild-type gene. The mutant also displayed a mutator phenotype. Our results provide insight into the allosteric regulation of the enzyme and support a physiologically important role of DNA binding.
-
-	Structure of Escherichia coli dGTP Triphosphohydrolase: A Hexameric Enzyme With DNA Effector Molecules.,Singh D, Gawel D, Itsko M, Hochkoeppler A, Krahn JM, London RE, Schaaper RM J Biol Chem. 2015 Feb 18. pii: jbc.M115.636936. PMID:25694425<ref>PMID:25694425</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4xds" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:24, 12 April 2023

OCA — Wed, 12 Apr 2023 21:24:38 GMT

←Older revision		Revision as of 21:24, 12 April 2023
Line 3:		Line 3:
	<StructureSection load='4xds' size='340' side='right'caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>		<StructureSection load='4xds' size='340' side='right'caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4xds]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4XDS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4xds]] is a 6 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=4XDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XDS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=NI:NICKEL+(II)+ION'>NI</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">dgt, b0160, JW0156 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [https://pdbe.org/4xds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [https://www.ebi.ac.uk/pdbsum/4xds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds 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/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [~~http~~://pdbe.org/4xds PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4xds PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI]] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>	+	[https://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: DGTPase]]~~	+	[[Category: Gawel D]]
-	[[Category: Gawel, D]]	+	[[Category: Itsko M]]
-	[[Category: Itsko, M]]	+	[[Category: Krahn JM]]
-	[[Category: Krahn~~, J M~~]]	+	[[Category: London RE]]
-	[[Category: London~~, R E~~]]	+	[[Category: Schaaper RM]]
-	[[Category: Schaaper~~, R M~~]]	+	[[Category: Singh D]]
-	[[Category: Singh, D]]	+
-	~~[[Category: Hydrolase-dna complex]]~~	+
-	~~[[Category: Triphosphohydrolase~~]]	+

OCA at 07:37, 29 May 2019

OCA — Wed, 29 May 2019 07:37:28 GMT

←Older revision		Revision as of 07:37, 29 May 2019
Line 1:		Line 1:

	==Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel==		==Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel==
-	<StructureSection load='4xds' size='340' side='right' caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>	+	<StructureSection load='4xds' size='340' side='right'caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4xds]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XDS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4xds]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XDS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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">dgt, b0160, JW0156 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [http://pdbe.org/4xds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [http://www.ebi.ac.uk/pdbsum/4xds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds ProSAT]</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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [http://pdbe.org/4xds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [http://www.ebi.ac.uk/pdbsum/4xds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds ProSAT]</span></td></tr>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: DGTPase]]		[[Category: DGTPase]]
	[[Category: Gawel, D]]		[[Category: Gawel, D]]

OCA at 18:47, 1 February 2017

OCA — Wed, 01 Feb 2017 18:47:53 GMT

←Older revision		Revision as of 18:47, 1 February 2017
Line 1:		Line 1:
		+
	==Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel==		==Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel==
	<StructureSection load='4xds' size='340' side='right' caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>		<StructureSection load='4xds' size='340' side='right' caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [http://www.ebi.ac.uk/pdbsum/4xds 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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [http://pdbe.org/4xds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [http://www.ebi.ac.uk/pdbsum/4xds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xds ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4xds" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:23, 4 March 2015

OCA — Wed, 04 Mar 2015 11:23:50 GMT

←Older revision		Revision as of 11:23, 4 March 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI]] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>		[[http://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI]] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The E. coli dgt gene encodes a dGTP triphosphohydrolase whose detailed role still remains to be determined. Deletion of dgt creates a mutator phenotype, indicating that the dGTPase has a fidelity role, possibly by affecting the cellular dNTP pool. In the present study, we have investigated the structure of Dgt protein at 3.1 A resolution. One of the obtained structures revealed a protein hexamer that contained two molecules of single-stranded DNA. The presence of DNA caused significant conformational changes in the enzyme, including in the enzyme's catalytic site. Dgt preparations lacking DNA were able to bind ssDNA with high affinity (Kd ~ 50 nM). DNA binding positively affected the enzyme's activity: dGTPase activity displayed sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP. A mutant Dgt enzyme was also created containing residue changes in the DNA binding cleft. This mutant enzyme, while still active, was incapable of DNA binding and could no longer be stimulated by addition of DNA. We also created an E. coli strain containing the mutant dgt gene on the chromosome replacing the wild-type gene. The mutant also displayed a mutator phenotype. Our results provide insight into the allosteric regulation of the enzyme and support a physiologically important role of DNA binding.
		+
		+	Structure of Escherichia coli dGTP Triphosphohydrolase: A Hexameric Enzyme With DNA Effector Molecules.,Singh D, Gawel D, Itsko M, Hochkoeppler A, Krahn JM, London RE, Schaaper RM J Biol Chem. 2015 Feb 18. pii: jbc.M115.636936. PMID:25694425<ref>PMID:25694425</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:06, 25 February 2015

OCA — Wed, 25 Feb 2015 14:06:50 GMT

←Older revision		Revision as of 14:06, 25 February 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel==
-		+	<StructureSection load='4xds' size='340' side='right' caption='[[4xds]], [[Resolution\|resolution]] 3.35Å' scene=''>
-	~~The entry~~ 4xds is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4xds]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XDS FirstGlance]. <br>
-	~~Authors~~: ~~Singh, D~~.~~, Gawel, D~~.~~, Itsko, M~~.~~, Krahn, J~~.M.~~, London, R~~.E.~~, Schaaper, R~~.M.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </span></td></tr>
-	~~Description~~: ~~Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel~~	+	<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=4xds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xds OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xds RCSB], [http://www.ebi.ac.uk/pdbsum/4xds PDBsum]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures]~~]	+	</table>
-	[[~~Category~~: ~~Schaaper~~, R.M]]	+	== Function ==
-	[[~~Category~~: ~~Itsko, M~~]]	+	[[http://www.uniprot.org/uniprot/DGTP_ECOLI DGTP_ECOLI]] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]<ref>PMID:2826481</ref>
-	[[Category: ~~London, R.E~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: DGTPase]]
	[[Category: Gawel, D]]		[[Category: Gawel, D]]
-	[[Category: Krahn, J.M]]	+	[[Category: Itsko, M]]
		+	[[Category: Krahn, J M]]
		+	[[Category: London, R E]]
		+	[[Category: Schaaper, R M]]
	[[Category: Singh, D]]		[[Category: Singh, D]]
		+	[[Category: Hydrolase-dna complex]]
		+	[[Category: Triphosphohydrolase]]

OCA at 11:15, 18 February 2015

OCA — Wed, 18 Feb 2015 11:15:48 GMT

←Older revision		Revision as of 11:15, 18 February 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M.		Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M.

OCA at 10:18, 12 February 2015

OCA — Thu, 12 Feb 2015 10:18:36 GMT

←Older revision		Revision as of 10:18, 12 February 2015
Line 5:		Line 5:
	Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M.		Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M.

-	Description: ~~DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE~~ from Escherichia coli with ~~two DNA effector molecules~~	+	Description: Deoxyguanosinetriphosphate Triphosphohydrolase from Escherichia coli with Nickel
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Schaaper, R.M]]		[[Category: Schaaper, R.M]]

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

OCA — Wed, 31 Dec 2014 14:01:56 GMT

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

←Older revision

Revision as of 14:01, 31 December 2014

OCA: New page: '''Unreleased structure''' The entry 4xds is ON HOLD Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M. Description: DEOXYGUANOSINETRIPHOSPHATE TRIPHOS...

OCA — Wed, 31 Dec 2014 14:01:55 GMT

New page: '''Unreleased structure''' The entry 4xds is ON HOLD Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M. Description: DEOXYGUANOSINETRIPHOSPHATE TRIPHOS...

New page

'''Unreleased structure'''

The entry 4xds is ON HOLD

Authors: Singh, D., Gawel, D., Itsko, M., Krahn, J.M., London, R.E., Schaaper, R.M.

Description: DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE from Escherichia coli with two DNA effector molecules
[[Category: Unreleased Structures]]
[[Category: Schaaper, R.M]]
[[Category: Itsko, M]]
[[Category: London, R.E]]
[[Category: Gawel, D]]
[[Category: Krahn, J.M]]
[[Category: Singh, D]]