2rt6 - Revision history

OCA at 10:04, 14 June 2023

2023-06-14T10:04:05Z

← Older revision		Revision as of 10:04, 14 June 2023
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	<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6]]' scene=''>		<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			In eubacterial organisms, the oriC-independent primosome plays an essential role in replication restart after the dissociation of the replication DNA-protein complex by DNA damage. PriC is a key protein component in the replication restart primosome. Our recent study suggested that PriC is divided into two domains: an N-terminal and a C-terminal domain. In the present study, we determined the solution structure of the N-terminal domain, whose structure and function have remained unknown until now. The revealed structure was composed of three helices and one extended loop. We also observed chemical shift changes in the heteronuclear NMR spectrum and oligomerization in the presence of ssDNA. These abilities may contribute to the PriC-ssDNA complex, which is important for the replication restart primosome.

			Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli.,Aramaki T, Abe Y, Katayama T, Ueda T Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2314. PMID:23868391<ref>PMID:23868391</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 2rt6" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Abe Y]]		[[Category: Abe Y]]

OCA at 10:25, 31 August 2022

2022-08-31T10:25:40Z

← Older revision		Revision as of 10:25, 31 August 2022
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	==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==		==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==
	<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>		<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[2rt6]] is a 1 chain structure.~~ Full ~~experimental~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></td></tr>
	</table>		</table>
	~~== Function ==~~
	[[https://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	In eubacterial organisms, the oriC-independent primosome plays an essential role in replication restart after the dissociation of the replication DNA-protein complex by DNA damage. PriC is a key protein component in the replication restart primosome. Our recent study suggested that PriC is divided into two domains: an N-terminal and a C-terminal domain. In the present study, we determined the solution structure of the N-terminal domain, whose structure and function have remained unknown until now. The revealed structure was composed of three helices and one extended loop. We also observed chemical shift changes in the heteronuclear NMR spectrum and oligomerization in the presence of ssDNA. These abilities may contribute to the PriC-ssDNA complex, which is important for the replication restart primosome.

	Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli.,Aramaki T, Abe Y, Katayama T, Ueda T Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2314. PMID:23868391<ref>PMID:23868391</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2rt6" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Abe, Y]]		[[Category: Abe Y]]
	[[Category: Aramaki, T]]		[[Category: Aramaki T]]
	[[Category: Katayama, T]]		[[Category: Katayama T]]
	[[Category: Ueda, T]]		[[Category: Ueda T]]
	~~[[Category: Dna binding protein]]~~
	~~[[Category: Pric]]~~
	~~[[Category: Primosome]]~~
	~~[[Category: Replication restart~~]]

OCA at 04:55, 25 August 2022

2022-08-25T04:55:52Z

← Older revision		Revision as of 04:55, 25 August 2022
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	<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure ~~with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0467, JW0456, priC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Ecoli]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Abe, Y]]		[[Category: Abe, Y]]

OCA at 10:36, 7 July 2021

2021-07-07T10:36:33Z

← Older revision		Revision as of 10:36, 7 July 2021
Line 1:		Line 1:

	==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==		==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==
	<StructureSection load='2rt6' size='340' side='right' caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rt6' size='340' side='right'caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0467, JW0456, priC ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0467, JW0456, priC ([https://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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [~~http~~://pdbe.org/2rt6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [https://pdbe.org/2rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.		[[https://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
			[[Category: Large Structures]]
	[[Category: Abe, Y]]		[[Category: Abe, Y]]
	[[Category: Aramaki, T]]		[[Category: Aramaki, T]]

OCA at 06:55, 5 August 2016

2016-08-05T06:55:35Z

← Older revision		Revision as of 06:55, 5 August 2016
Line 1:		Line 1:

	==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==		==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==
	<StructureSection load='2rt6' size='340' side='right' caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rt6' size='340' side='right' caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12 Escherichia coli k-12~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0467, JW0456, priC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0467, JW0456, priC ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt6 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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [http://pdbe.org/2rt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 2rt6" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Escherichia coli k-12~~]]		[[Category: Ecoli]]
	[[Category: Abe, Y]]		[[Category: Abe, Y]]
	[[Category: Aramaki, T]]		[[Category: Aramaki, T]]

OCA at 16:40, 25 December 2014

2014-12-25T16:40:37Z

← Older revision		Revision as of 16:40, 25 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2rt6\| PDB=2rt6 \| SCENE= }}~~		==Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain==
	===Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain===		<StructureSection load='2rt6' size='340' side='right' caption='[[2rt6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	~~{{ABSTRACT_PUBMED_23868391}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2rt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RT6 FirstGlance]. <br>
	==Function==		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0467, JW0456, priC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=2rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rt6 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt6 PDBsum]</span></td></tr>
			</table>
			== Function ==
	[[http://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.		[[http://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			In eubacterial organisms, the oriC-independent primosome plays an essential role in replication restart after the dissociation of the replication DNA-protein complex by DNA damage. PriC is a key protein component in the replication restart primosome. Our recent study suggested that PriC is divided into two domains: an N-terminal and a C-terminal domain. In the present study, we determined the solution structure of the N-terminal domain, whose structure and function have remained unknown until now. The revealed structure was composed of three helices and one extended loop. We also observed chemical shift changes in the heteronuclear NMR spectrum and oligomerization in the presence of ssDNA. These abilities may contribute to the PriC-ssDNA complex, which is important for the replication restart primosome.

	~~==About this Structure==~~		Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli.,Aramaki T, Abe Y, Katayama T, Ueda T Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2314. PMID:23868391<ref>PMID:23868391</ref>
	~~[[2rt6]] is a 1 chain~~ structure ~~with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k~~-12 Escherichia coli ~~k-12]~~. ~~Full experimental information is available from [http~~:/~~/oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=2RT6 OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:023868391</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: Abe, Y.]]		[[Category: Abe, Y]]
	[[Category: Aramaki, T.]]		[[Category: Aramaki, T]]
	[[Category: Katayama, T.]]		[[Category: Katayama, T]]
	[[Category: Ueda, T.]]		[[Category: Ueda, T]]
	[[Category: Dna binding protein]]		[[Category: Dna binding protein]]
	[[Category: Pric]]		[[Category: Pric]]
	[[Category: Primosome]]		[[Category: Primosome]]
	[[Category: Replication restart]]		[[Category: Replication restart]]

OCA at 20:56, 7 August 2013

2013-08-07T20:56:49Z

← Older revision		Revision as of 20:56, 7 August 2013
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		{{STRUCTURE_2rt6\| PDB=2rt6 \| SCENE= }}
			===Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain===
			{{ABSTRACT_PUBMED_23868391}}

	~~The entry 2rt6~~ is ~~ON HOLD until Paper Publication~~		==Function==
			[[http://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.

	~~Authors~~: ~~Aramaki, T~~.~~, Abe, Y~~.~~, Katayama, T~~.~~, Ueda, T~~.		==About this Structure==
			[[2rt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA].

	~~Description~~: ~~Backbone 1H~~, ~~13C~~, ~~and 15N Chemical Shift Assignments for PriC N-terminal domain~~		==Reference==
			<ref group="xtra">PMID:023868391</ref><references group="xtra"/><references/>
			[[Category: Escherichia coli k-12]]
			[[Category: Abe, Y.]]
			[[Category: Aramaki, T.]]
			[[Category: Katayama, T.]]
			[[Category: Ueda, T.]]
			[[Category: Dna binding protein]]
			[[Category: Pric]]
			[[Category: Primosome]]
			[[Category: Replication restart]]

OCA: Protected "2rt6" [edit=sysop:move=sysop]

2013-06-19T10:32:41Z

Protected "2rt6" [edit=sysop:move=sysop]

← Older revision	Revision as of 10:32, 19 June 2013
(No difference)

OCA: New page: '''Unreleased structure''' The entry 2rt6 is ON HOLD until Paper Publication Authors: Aramaki, T., Abe, Y., Katayama, T., Ueda, T. Description: Backbone 1H, 13C, and 15N Chemical Shift...

2013-06-19T10:32:40Z

New page: '''Unreleased structure''' The entry 2rt6 is ON HOLD until Paper Publication Authors: Aramaki, T., Abe, Y., Katayama, T., Ueda, T. Description: Backbone 1H, 13C, and 15N Chemical Shift...

New page

'''Unreleased structure'''

The entry 2rt6 is ON HOLD until Paper Publication

Authors: Aramaki, T., Abe, Y., Katayama, T., Ueda, T.

Description: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain