4k74 - Revision history

OCA at 15:54, 20 September 2023

OCA — Wed, 20 Sep 2023 15:54:35 GMT

←Older revision		Revision as of 15:54, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4k74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K74 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4k74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K74 FirstGlance]. <br>
-	</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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [https://pdbe.org/4k74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [https://www.ebi.ac.uk/pdbsum/4k74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k74 ProSAT]</span></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]] 2.5Å</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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [https://pdbe.org/4k74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [https://www.ebi.ac.uk/pdbsum/4k74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k74 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4k74" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4k74" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:43, 30 November 2022

OCA — Wed, 30 Nov 2022 11:43:08 GMT

←Older revision		Revision as of 11:43, 30 November 2022
Line 1:		Line 1:

	==The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.==		==The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.==
-	<StructureSection load='4k74' size='340' side='right' caption='[[4k74]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4k74' size='340' side='right'caption='[[4k74]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k74]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K74 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4K74 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K74 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>	+	</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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [https://pdbe.org/4k74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [https://www.ebi.ac.uk/pdbsum/4k74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k74 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/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [~~http~~://pdbe.org/4k74 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4k74 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4k74 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/Q1R4N6_ECOUT Q1R4N6_ECOUT]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity).[PIRNR:PIRNR000804]	+	[https://www.uniprot.org/uniprot/Q1R4N6_ECOUT Q1R4N6_ECOUT] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity).[PIRNR:PIRNR000804]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4k74" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4k74" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[DNA polymerase\|DNA polymerase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
-	[[Category: ~~DNA-directed DNA polymerase~~]]	+	[[Category: Large Structures]]
-	[[Category: Bunting~~, K A~~]]	+	[[Category: Bunting KA]]
-	[[Category: Patoli~~, A A~~]]	+	[[Category: Patoli AA]]
-	[[Category: Winter~~, J A]]~~	+	[[Category: Winter JA]]
-	~~[[Category: Dna binding protein-transferase complex]]~~	+
-	~~[[Category: Dna replication clamp processivity factor]]~~	+
-	~~[[Category: Dna replication/repair~~]]	+

OCA at 20:38, 4 August 2016

OCA — Thu, 04 Aug 2016 20:38:29 GMT

←Older revision		Revision as of 20:38, 4 August 2016
Line 1:		Line 1:
		+
	==The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.==		==The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.==
	<StructureSection load='4k74' size='340' side='right' caption='[[4k74]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4k74' size='340' side='right' caption='[[4k74]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k74]] 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=4K74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K74 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K74 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 ~~Escherichia~~ coli])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [http://www.ebi.ac.uk/pdbsum/4k74 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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [http://pdbe.org/4k74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [http://www.ebi.ac.uk/pdbsum/4k74 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k74 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 4k74" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus coli migula 1895]]
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
-	[[Category: Escherichia coli]]
	[[Category: Bunting, K A]]		[[Category: Bunting, K A]]
	[[Category: Patoli, A A]]		[[Category: Patoli, A A]]

OCA at 12:57, 25 December 2014

OCA — Thu, 25 Dec 2014 12:57:39 GMT

←Older revision		Revision as of 12:57, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4k74\| PDB=4k74 \| SCENE= }}~~	+	==The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.==
-	===The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.===	+	<StructureSection load='4k74' size='340' side='right' caption='[[4k74]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23822808}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4k74]] 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=4K74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K74 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dnaN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4k74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k74 RCSB], [http://www.ebi.ac.uk/pdbsum/4k74 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/Q1R4N6_ECOUT Q1R4N6_ECOUT]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity).[PIRNR:PIRNR000804]		[[http://www.uniprot.org/uniprot/Q1R4N6_ECOUT Q1R4N6_ECOUT]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity).[PIRNR:PIRNR000804]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: Strict regulation of replisome components is essential to ensure the accurate transmission of the genome to the next generation. The sliding clamp processivity factors play a central role in this regulation, interacting with both DNA polymerases and multiple DNA processing and repair proteins. Clamp binding partners share a common peptide binding motif, the nature of which is essentially conserved from phage through to humans. Given the degree of conservation of these motifs, much research effort has focussed on understanding how the temporal and spatial regulation of multiple clamp binding partners is managed. The bacterial sliding clamps have come under scrutiny as potential targets for rational drug design and comprehensive understanding of the structural basis of their interactions is crucial for success. RESULTS: In this study we describe the crystal structure of a complex of the E. coli beta-clamp with a 12-mer peptide from the UmuC protein. UmuC is the catalytic subunit of the translesion DNA polymerase, Pol V (UmuD'2C). Due to its potentially mutagenic action, Pol V is tightly regulated in the cell to limit access to the replication fork. Atypically for the translesion polymerases, both bacterial and eukaryotic, Pol V is heterotrimeric and its beta-clamp binding motif (357 QLNLF 361) is internal to the protein, rather than at the more usual C-terminal position. Our structure shows that the UmuC peptide follows the overall disposition of previously characterised structures with respect to the highly conserved glutamine residue. Despite good agreement with the consensus beta-clamp binding motif, distinct variation is shown within the hydrophobic binding pocket. While UmuC Leu-360 interacts as noted in other structures, Phe-361 does not penetrate the pocket at all, sitting above the surface. CONCLUSION: Although the beta-clamp binding motif of UmuC conforms to the consensus sequence, variation in its mode of clamp binding is observed compared to related structures, presumably dictated by the proximal aspartate residues that act as linker to the poorly characterised, unique C-terminal domain of UmuC. Additionally, interactions between Asn-359 of UmuC and Arg-152 on the clamp surface may compensate for the reduced interaction of Phe-361.
		+
		+	The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.,Patoli AA, Winter JA, Bunting KA BMC Struct Biol. 2013 Jul 4;13(1):12. PMID:23822808<ref>PMID:23822808</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4k74]] 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=4K74 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023822808</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[DNA polymerase\|DNA polymerase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Bunting, K A.]]	+	[[Category: Bunting, K A]]
-	[[Category: Patoli, A A.]]	+	[[Category: Patoli, A A]]
-	[[Category: Winter, J A.]]	+	[[Category: Winter, J A]]
	[[Category: Dna binding protein-transferase complex]]		[[Category: Dna binding protein-transferase complex]]
	[[Category: Dna replication clamp processivity factor]]		[[Category: Dna replication clamp processivity factor]]
	[[Category: Dna replication/repair]]		[[Category: Dna replication/repair]]

OCA at 04:54, 18 July 2013

OCA — Thu, 18 Jul 2013 04:54:16 GMT

←Older revision		Revision as of 04:54, 18 July 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4k74\| PDB=4k74 \| SCENE= }}
		+	===The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.===
		+	{{ABSTRACT_PUBMED_23822808}}

-	The ~~entry 4k74~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/Q1R4N6_ECOUT Q1R4N6_ECOUT]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity).[PIRNR:PIRNR000804]

-	~~Authors~~: ~~Patoli, A~~.A.~~, Winter, J~~.A.~~, Bunting, K~~.A.	+	==About this Structure==
		+	[[4k74]] 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=4K74 OCA].

-	~~Description~~: ~~The UmuC subunit of the E. coli~~ DNA polymerase ~~V shows a unique interaction with the beta~~-clamp processivity factor.	+	==Reference==
		+	<ref group="xtra">PMID:023822808</ref><references group="xtra"/><references/>
		+	[[Category: DNA-directed DNA polymerase]]
		+	[[Category: Escherichia coli]]
		+	[[Category: Bunting, K A.]]
		+	[[Category: Patoli, A A.]]
		+	[[Category: Winter, J A.]]
		+	[[Category: Dna binding protein-transferase complex]]
		+	[[Category: Dna replication clamp processivity factor]]
		+	[[Category: Dna replication/repair]]

OCA at 07:12, 2 May 2013

OCA — Thu, 02 May 2013 07:12:12 GMT

←Older revision		Revision as of 07:12, 2 May 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4k74 is ON HOLD	+	The entry 4k74 is ON HOLD until Paper Publication

	Authors: Patoli, A.A., Winter, J.A., Bunting, K.A.		Authors: Patoli, A.A., Winter, J.A., Bunting, K.A.

	Description: The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.		Description: The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.

OCA: Protected "4k74" [edit=sysop:move=sysop]

OCA — Wed, 24 Apr 2013 11:01:28 GMT

Protected "4k74" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:01, 24 April 2013

OCA: New page: '''Unreleased structure''' The entry 4k74 is ON HOLD Authors: Patoli, A.A., Winter, J.A., Bunting, K.A. Description: The UmuC subunit of the E. coli DNA polymerase V shows a unique int...

OCA — Wed, 24 Apr 2013 11:01:27 GMT

New page: '''Unreleased structure''' The entry 4k74 is ON HOLD Authors: Patoli, A.A., Winter, J.A., Bunting, K.A. Description: The UmuC subunit of the E. coli DNA polymerase V shows a unique int...

New page

'''Unreleased structure'''

The entry 4k74 is ON HOLD

Authors: Patoli, A.A., Winter, J.A., Bunting, K.A.

Description: The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.