4xus - Revision history

OCA at 13:01, 1 March 2024

2024-03-01T13:01:46Z

← Older revision		Revision as of 13:01, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4xus]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XUS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4xus]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XUS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</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]] 2.4Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [https://pdbe.org/4xus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [https://www.ebi.ac.uk/pdbsum/4xus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xus 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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [https://pdbe.org/4xus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [https://www.ebi.ac.uk/pdbsum/4xus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xus ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>		[https://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	8-Oxo-7,8,-dihydro-2'-deoxyguanosine triphosphate (8-oxo-dGTP) is a major product of oxidative damage in the nucleotide pool. It is capable of mispairing with adenosine (dA), resulting in futile, mutagenic cycles of base excision repair. Therefore, it is critical that DNA polymerases discriminate against 8-oxo-dGTP at the insertion step. Because of its roles in oxidative DNA damage repair and non-homologous end joining, DNA polymerase lambda (Pol lambda) may frequently encounter 8-oxo-dGTP. Here, we have studied the mechanisms of 8-oxo-dGMP incorporation and discrimination by Pol lambda. We have solved high resolution crystal structures showing how Pol lambda accommodates 8-oxo-dGTP in its active site. The structures indicate that when mispaired with dA, the oxidized nucleotide assumes the mutagenic syn-conformation, and is stabilized by multiple interactions. Steady-state kinetics reveal that two residues lining the dNTP binding pocket, Ala(510) and Asn(513), play differential roles in dNTP selectivity. Specifically, Ala(510) and Asn(513) facilitate incorporation of 8-oxo-dGMP opposite dA and dC, respectively. These residues also modulate the balance between purine and pyrimidine incorporation. Our results shed light on the mechanisms controlling 8-oxo-dGMP incorporation in Pol lambda and on the importance of interactions with the incoming dNTP to determine selectivity in family X DNA polymerases.

	Nucleotide binding interactions modulate dNTP selectivity and facilitate 8-oxo-dGTP incorporation by DNA polymerase lambda.,Burak MJ, Guja KE, Garcia-Diaz M Nucleic Acids Res. 2015 Sep 18;43(16):8089-99. doi: 10.1093/nar/gkv760. Epub 2015, Jul 28. PMID:26220180<ref>PMID:26220180</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4xus" style="background-color:#fffaf0;"></div>~~

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

OCA at 17:53, 26 April 2023

2023-04-26T17:53:28Z

← Older revision		Revision as of 17:53, 26 April 2023
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	<StructureSection load='4xus' size='340' side='right'caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4xus' size='340' side='right'caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4xus]] is a 4 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=4XUS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4XUS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4xus]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XUS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POLL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [https://pdbe.org/4xus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [https://www.ebi.ac.uk/pdbsum/4xus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xus 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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [~~http~~://pdbe.org/4xus PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4xus PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4xus ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN]] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>		[https://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4xus" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4xus" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Burak, M J~~]]		[[Category: Synthetic construct]]
	[[Category: ~~Garcia-Diaz, M~~]]		[[Category: Burak MJ]]
	[[Category: ~~Guja, K E]]~~		[[Category: Garcia-Diaz M]]
	~~[[Category: Dna polymerase lambda]]~~		[[Category: Guja KE]]
	~~[[Category: Helix~~-~~hairpin-helix~~]]
	[[Category: ~~Protein-dna complex]]~~
	~~[[Category: Transferase-dna complex~~]]

OCA at 23:29, 5 June 2019

2019-06-05T23:29:03Z

← Older revision		Revision as of 23:29, 5 June 2019
Line 1:		Line 1:

	==Crystal structure of the pre-catalytic ternary complex of DNA polymerase lambda with a templating A and an incoming dTTP==		==Crystal structure of the pre-catalytic ternary complex of DNA polymerase lambda with a templating A and an incoming dTTP==
	<StructureSection load='4xus' size='340' side='right' caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4xus' size='340' side='right'caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4xus]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XUS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4xus]] is a 4 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=4XUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XUS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [http://pdbe.org/4xus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [http://www.ebi.ac.uk/pdbsum/4xus PDBsum]</span></td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POLL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [http://pdbe.org/4xus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [http://www.ebi.ac.uk/pdbsum/4xus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xus ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Burak, M J]]		[[Category: Burak, M J]]
	[[Category: Garcia-Diaz, M]]		[[Category: Garcia-Diaz, M]]

OCA at 09:01, 10 February 2016

2016-02-10T09:01:11Z

← Older revision		Revision as of 09:01, 10 February 2016
Line 1:		Line 1:
	==Crystal structure of the pre-catalytic ternary complex of DNA polymerase lambda with a templating A and an incoming ~~8-oxo-dGTP~~==		==Crystal structure of the pre-catalytic ternary complex of DNA polymerase lambda with a templating A and an incoming dTTP==
	<StructureSection load='4xus' size='340' side='right' caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4xus' size='340' side='right' caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN]] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>		[[http://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN]] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			8-Oxo-7,8,-dihydro-2'-deoxyguanosine triphosphate (8-oxo-dGTP) is a major product of oxidative damage in the nucleotide pool. It is capable of mispairing with adenosine (dA), resulting in futile, mutagenic cycles of base excision repair. Therefore, it is critical that DNA polymerases discriminate against 8-oxo-dGTP at the insertion step. Because of its roles in oxidative DNA damage repair and non-homologous end joining, DNA polymerase lambda (Pol lambda) may frequently encounter 8-oxo-dGTP. Here, we have studied the mechanisms of 8-oxo-dGMP incorporation and discrimination by Pol lambda. We have solved high resolution crystal structures showing how Pol lambda accommodates 8-oxo-dGTP in its active site. The structures indicate that when mispaired with dA, the oxidized nucleotide assumes the mutagenic syn-conformation, and is stabilized by multiple interactions. Steady-state kinetics reveal that two residues lining the dNTP binding pocket, Ala(510) and Asn(513), play differential roles in dNTP selectivity. Specifically, Ala(510) and Asn(513) facilitate incorporation of 8-oxo-dGMP opposite dA and dC, respectively. These residues also modulate the balance between purine and pyrimidine incorporation. Our results shed light on the mechanisms controlling 8-oxo-dGMP incorporation in Pol lambda and on the importance of interactions with the incoming dNTP to determine selectivity in family X DNA polymerases.

			Nucleotide binding interactions modulate dNTP selectivity and facilitate 8-oxo-dGTP incorporation by DNA polymerase lambda.,Burak MJ, Guja KE, Garcia-Diaz M Nucleic Acids Res. 2015 Sep 18;43(16):8089-99. doi: 10.1093/nar/gkv760. Epub 2015, Jul 28. PMID:26220180<ref>PMID:26220180</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4xus" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:50, 3 February 2016

2016-02-03T15:50:20Z

← Older revision		Revision as of 15:50, 3 February 2016
Line 1:		Line 1:
	'''~~Unreleased structure~~'''		==Crystal structure of the pre-catalytic ternary complex of DNA polymerase lambda with a templating A and an incoming 8-oxo-dGTP==
			<StructureSection load='4xus' size='340' side='right' caption='[[4xus]], [[Resolution\|resolution]] 2.40Å' scene=''>
	~~The entry~~ 4xus is ~~ON HOLD until Feb 03 2017~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4xus]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XUS FirstGlance]. <br>
	~~Authors~~: ~~Burak~~, M.J., ~~Guja~~, K.E., ~~Garcia-Diaz, M~~.		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></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=4xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xus OCA], [http://pdbe.org/4xus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xus RCSB], [http://www.ebi.ac.uk/pdbsum/4xus PDBsum]</span></td></tr>
	~~Description~~: ~~Crystal structure of the pre-catalytic ternary complex~~ of DNA polymerase ~~lambda with~~ a ~~templating A and an incoming 8~~-~~oxo~~-~~dGTP~~		</table>
	~~[[Category: Unreleased Structures]]~~		== Function ==
	[[Category: ~~Guja~~, ~~K.E~~]]		[[http://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN]] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Burak, M J]]
	[[Category: Garcia-Diaz, M]]		[[Category: Garcia-Diaz, M]]
	[[Category: ~~Burak~~, ~~M.J~~]]		[[Category: Guja, K E]]
			[[Category: Dna polymerase lambda]]
			[[Category: Helix-hairpin-helix]]
			[[Category: Protein-dna complex]]
			[[Category: Transferase-dna complex]]

OCA at 19:30, 27 January 2016

2016-01-27T19:30:32Z

← Older revision		Revision as of 19:30, 27 January 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4xus is ON HOLD until ~~Jan 26~~ 2017		The entry 4xus is ON HOLD until Feb 03 2017

	Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M.		Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M.

OCA at 23:20, 30 November 2015

2015-11-30T23:20:33Z

← Older revision		Revision as of 23:20, 30 November 2015
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Guja, K.E]]		[[Category: Guja, K.E]]
			[[Category: Garcia-Diaz, M]]
	[[Category: Burak, M.J]]		[[Category: Burak, M.J]]
	~~[[Category: Garcia-Diaz, M]]~~

OCA at 09:50, 4 March 2015

2015-03-04T09:50:18Z

← Older revision		Revision as of 09:50, 4 March 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4xus is ON HOLD		The entry 4xus is ON HOLD until Jan 26 2017

	Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M.		Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M.

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

2015-02-07T14:50:57Z

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

← Older revision	Revision as of 14:50, 7 February 2015
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4xus is ON HOLD Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M. Description: Crystal structure of the pre-catalytic ternary complex of DNA polyme...

2015-02-07T14:50:56Z

New page: '''Unreleased structure''' The entry 4xus is ON HOLD Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M. Description: Crystal structure of the pre-catalytic ternary complex of DNA polyme...

New page

'''Unreleased structure'''

The entry 4xus is ON HOLD

Authors: Burak, M.J., Guja, K.E., Garcia-Diaz, M.

Description: Crystal structure of the pre-catalytic ternary complex of DNA polymerase lambda with a templating A and an incoming 8-oxo-dGTP
[[Category: Unreleased Structures]]
[[Category: Guja, K.E]]
[[Category: Burak, M.J]]
[[Category: Garcia-Diaz, M]]