4m9n - Revision history

OCA at 12:24, 1 March 2024

OCA — Fri, 01 Mar 2024 12:24:59 GMT

←Older revision		Revision as of 12:24, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4m9n]] is a 4 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=4M9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M9N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4m9n]] is a 4 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=4M9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M9N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.275Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [https://pdbe.org/4m9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [https://www.ebi.ac.uk/pdbsum/4m9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m9n 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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [https://pdbe.org/4m9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [https://www.ebi.ac.uk/pdbsum/4m9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m9n ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>		[https://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DNA polymerase beta (pol beta) is responsible for gap filling synthesis during repair of damaged DNA as part of the base excision repair pathway. Human pol beta mutations were recently identified in a high percentage (~30%) of tumors. Characterization of specific cancer variants is particularly useful to further the understanding of the general mechanism of pol beta while providing context to disease contribution. We showed that expression of the carcinoma variant E295K induces cellular transformation. The poor polymerase activity exhibited by the variant was hypothesized to be caused by the destabilization of proper active site assembly by the glutamate to lysine mutation. Here we show that this variant exhibits an unusual preference for binding dCTP opposite a templating adenine over the cognate dTTP. Biochemical studies indicate that the non-cognate competes with the cognate nucleotide for binding to the polymerase active site with the non-cognate incorporation a function of higher affinity and not increased activity. In the crystal structure of the variant bound to dA:dCTP, the fingers domain closes around the mismatched base pair. Nucleotide incorporation is hindered because key residues in the polymerase active site are not properly positioned for nucleotidyl transfer. In contrast to the non-cognate dCTP, neither the cognate dTTP nor its non-hydrolyzable analog induced fingers closure, as isomorphous difference Fourier maps show that the cognate nucleotides are bound to the open state of the polymerase. Comparison to published structures provides insight into the structural rearrangements within pol beta that occur during the process of nucleotide discrimination.

-	The E295K cancer variant of human polymerase beta favors the mismatch conformational pathway during nucleotide selection.,Eckenroth BE, Towle-Weicksel JB, Sweasy JB, Doublie S J Biol Chem. 2013 Oct 18. PMID:24133209<ref>PMID:24133209</ref>	+	==See Also==
-		+	*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 4m9n" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:04, 21 December 2022

OCA — Wed, 21 Dec 2022 11:04:36 GMT

←Older revision		Revision as of 11:04, 21 December 2022
Line 1:		Line 1:

	==DNA Polymerase Beta E295K Soaked with dATP==		==DNA Polymerase Beta E295K Soaked with dATP==
-	<StructureSection load='4m9n' size='340' side='right' caption='[[4m9n]], [[Resolution\|resolution]] 2.27Å' scene=''>	+	<StructureSection load='4m9n' size='340' side='right'caption='[[4m9n]], [[Resolution\|resolution]] 2.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m9n]] 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=4M9N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4M9N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4m9n]] is a 4 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=4M9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M9N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m9g\|4m9g]], [[4m9h\|4m9h]], [[4m9j\|4m9j]], [[4m9l\|4m9l]]</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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [https://pdbe.org/4m9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [https://www.ebi.ac.uk/pdbsum/4m9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m9n ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POLB ([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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [~~http~~://pdbe.org/4m9n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4m9n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4m9n ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>	+	[https://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4m9n" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4m9n" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[DNA polymerase\|DNA polymerase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Doublie, S~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Eckenroth, B E~~]]	+	[[Category: Doublie S]]
-	[[Category: ~~Dna complex]]~~	+	[[Category: Eckenroth BE]]
-	~~[[Category: Dna polymerase]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Transferase-dna complex~~]]	+

OCA at 11:16, 4 August 2016

OCA — Thu, 04 Aug 2016 11:16:40 GMT

←Older revision		Revision as of 11:16, 4 August 2016
Line 1:		Line 1:
		+
	==DNA Polymerase Beta E295K Soaked with dATP==		==DNA Polymerase Beta E295K Soaked with dATP==
	<StructureSection load='4m9n' size='340' side='right' caption='[[4m9n]], [[Resolution\|resolution]] 2.27Å' scene=''>		<StructureSection load='4m9n' size='340' side='right' caption='[[4m9n]], [[Resolution\|resolution]] 2.27Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m9g\|4m9g]], [[4m9h\|4m9h]], [[4m9j\|4m9j]], [[4m9l\|4m9l]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m9g\|4m9g]], [[4m9h\|4m9h]], [[4m9j\|4m9j]], [[4m9l\|4m9l]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POLB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POLB ([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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [http://www.ebi.ac.uk/pdbsum/4m9n 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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [http://pdbe.org/4m9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [http://www.ebi.ac.uk/pdbsum/4m9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m9n 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 4m9n" style="background-color:#fffaf0;"></div>

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

OCA at 13:46, 24 December 2014

OCA — Wed, 24 Dec 2014 13:46:11 GMT

←Older revision		Revision as of 13:46, 24 December 2014
Line 8:		Line 8:
	<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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [http://www.ebi.ac.uk/pdbsum/4m9n 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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [http://www.ebi.ac.uk/pdbsum/4m9n PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:10, 21 December 2014

OCA — Sun, 21 Dec 2014 18:10:29 GMT

←Older revision		Revision as of 18:10, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4m9n\| PDB=4m9n \| SCENE= }}~~	+	==DNA Polymerase Beta E295K Soaked with dATP==
-	===DNA Polymerase Beta E295K Soaked with dATP===	+	<StructureSection load='4m9n' size='340' side='right' caption='[[4m9n]], [[Resolution\|resolution]] 2.27Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24133209}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4m9n]] 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=4M9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M9N FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m9g\|4m9g]], [[4m9h\|4m9h]], [[4m9j\|4m9j]], [[4m9l\|4m9l]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POLB ([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=4m9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m9n RCSB], [http://www.ebi.ac.uk/pdbsum/4m9n PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DNA polymerase beta (pol beta) is responsible for gap filling synthesis during repair of damaged DNA as part of the base excision repair pathway. Human pol beta mutations were recently identified in a high percentage (~30%) of tumors. Characterization of specific cancer variants is particularly useful to further the understanding of the general mechanism of pol beta while providing context to disease contribution. We showed that expression of the carcinoma variant E295K induces cellular transformation. The poor polymerase activity exhibited by the variant was hypothesized to be caused by the destabilization of proper active site assembly by the glutamate to lysine mutation. Here we show that this variant exhibits an unusual preference for binding dCTP opposite a templating adenine over the cognate dTTP. Biochemical studies indicate that the non-cognate competes with the cognate nucleotide for binding to the polymerase active site with the non-cognate incorporation a function of higher affinity and not increased activity. In the crystal structure of the variant bound to dA:dCTP, the fingers domain closes around the mismatched base pair. Nucleotide incorporation is hindered because key residues in the polymerase active site are not properly positioned for nucleotidyl transfer. In contrast to the non-cognate dCTP, neither the cognate dTTP nor its non-hydrolyzable analog induced fingers closure, as isomorphous difference Fourier maps show that the cognate nucleotides are bound to the open state of the polymerase. Comparison to published structures provides insight into the structural rearrangements within pol beta that occur during the process of nucleotide discrimination.

-	~~==Function==~~	+	The E295K cancer variant of human polymerase beta favors the mismatch conformational pathway during nucleotide selection.,Eckenroth BE, Towle-Weicksel JB, Sweasy JB, Doublie S J Biol Chem. 2013 Oct 18. PMID:24133209<ref>PMID:24133209</ref>
-	~~[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair~~ polymerase ~~that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes~~ the ~~5' sugar phosphate and also acts as a DNA polymerase that adds one~~ nucleotide ~~to the 3' end of the arising single-nucleotide gap~~. ~~Conducts 'gap~~-~~filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases~~.~~<ref>~~PMID:~~9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref>~~ <ref>PMID:~~21362556~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4m9n]] 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=4M9N OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:024133209</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[DNA polymerase\|DNA polymerase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Doublie, S.]]	+	[[Category: Doublie, S]]
-	[[Category: Eckenroth, B E.]]	+	[[Category: Eckenroth, B E]]
	[[Category: Dna complex]]		[[Category: Dna complex]]
	[[Category: Dna polymerase]]		[[Category: Dna polymerase]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Transferase-dna complex]]		[[Category: Transferase-dna complex]]

OCA at 08:17, 18 December 2013

OCA — Wed, 18 Dec 2013 08:17:03 GMT

←Older revision		Revision as of 08:17, 18 December 2013
Line 7:		Line 7:

	==About this Structure==		==About this Structure==
-	[[4m9n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M9N OCA].	+	[[4m9n]] 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=4M9N OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024133209</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024133209</ref><references group="xtra"/><references/>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Doublie, S.]]		[[Category: Doublie, S.]]
	[[Category: Eckenroth, B E.]]		[[Category: Eckenroth, B E.]]

OCA at 08:34, 30 October 2013

OCA — Wed, 30 Oct 2013 08:34:12 GMT

←Older revision		Revision as of 08:34, 30 October 2013
Line 1:		Line 1:
	{{STRUCTURE_4m9n\| PDB=4m9n \| SCENE= }}		{{STRUCTURE_4m9n\| PDB=4m9n \| SCENE= }}
	===DNA Polymerase Beta E295K Soaked with dATP===		===DNA Polymerase Beta E295K Soaked with dATP===
		+	{{ABSTRACT_PUBMED_24133209}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024133209</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Doublie, S.]]		[[Category: Doublie, S.]]

OCA at 08:11, 16 October 2013

OCA — Wed, 16 Oct 2013 08:11:02 GMT

←Older revision		Revision as of 08:11, 16 October 2013
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-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4m9n\| PDB=4m9n \| SCENE= }}
		+	===DNA Polymerase Beta E295K Soaked with dATP===

-	~~The entry 4m9n is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>

-	~~Authors~~: ~~Eckenroth, B~~.E.~~, Doublie, S~~.	+	==About this Structure==
		+	[[4m9n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M9N OCA].

-	~~Description~~:	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Doublie, S.]]
		+	[[Category: Eckenroth, B E.]]
		+	[[Category: Dna complex]]
		+	[[Category: Dna polymerase]]
		+	[[Category: Lyase]]
		+	[[Category: Transferase-dna complex]]

OCA at 09:59, 4 September 2013

OCA — Wed, 04 Sep 2013 09:59:59 GMT

←Older revision		Revision as of 09:59, 4 September 2013
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	Authors: Eckenroth, B.E., Doublie, S.		Authors: Eckenroth, B.E., Doublie, S.

-	Description: ~~E295K soaked with dATP~~	+	Description:

OCA: Protected "4m9n" [edit=sysop:move=sysop]

OCA — Wed, 21 Aug 2013 08:00:12 GMT

Protected "4m9n" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:00, 21 August 2013