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2pnh

From Proteopedia

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Escherichia coli PriB E39A variant

Structural highlights

2pnh is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.25Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRIB_ECOLI Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Collapsed DNA replication forks must be reactivated through origin-independent reloading of the replication machinery (replisome) to ensure complete duplication of cellular genomes. In E. coli, the PriA-dependent pathway is the major replication restart mechanism and requires primosome proteins PriA, PriB, and DnaT for replisome reloading. However, the molecular mechanisms that regulate origin-independent replisome loading are not fully understood. Here, we demonstrate that assembly of primosome protein complexes represents a key regulatory mechanism, as inherently weak PriA-PriB and PriB-DnaT interactions are strongly stimulated by single-stranded DNA. Furthermore, the binding site on PriB for single-stranded DNA partially overlaps the binding sites for PriA and DnaT, suggesting a dynamic primosome assembly process in which single-stranded DNA is handed off from one primosome protein to another as a repaired replication fork is reactivated. This model helps explain how origin-independent initiation of DNA replication is restricted to repaired replication forks, preventing overreplication of the genome.

A hand-off mechanism for primosome assembly in replication restart.,Lopper M, Boonsombat R, Sandler SJ, Keck JL Mol Cell. 2007 Jun 22;26(6):781-93. PMID:17588514^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zavitz KH, DiGate RJ, Marians KJ. The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification. J Biol Chem. 1991 Jul 25;266(21):13988-95. PMID:1856227
↑ Allen GC Jr, Kornberg A. The priB gene encoding the primosomal replication n protein of Escherichia coli. J Biol Chem. 1991 Jun 25;266(18):11610-3. PMID:1646811
↑ Allen GC Jr, Kornberg A. Assembly of the primosome of DNA replication in Escherichia coli. J Biol Chem. 1993 Sep 15;268(26):19204-9. PMID:8366072
↑ Lopper M, Boonsombat R, Sandler SJ, Keck JL. A hand-off mechanism for primosome assembly in replication restart. Mol Cell. 2007 Jun 22;26(6):781-93. PMID:17588514 doi:10.1016/j.molcel.2007.05.012

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pnh"

Categories: Escherichia coli K-12 | Large Structures | Keck JL | Lopper ME

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2pnh.png|left|200px]]
-<!--
+==Escherichia coli PriB E39A variant==
-The line below this paragraph, containing "STRUCTURE_2pnh", creates the "Structure Box" on the page.
+<StructureSection load='2pnh' size='340' side='right'caption='[[2pnh]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2pnh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</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=2pnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pnh OCA], [https://pdbe.org/2pnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pnh RCSB], [https://www.ebi.ac.uk/pdbsum/2pnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pnh ProSAT]</span></td></tr>
-{{STRUCTURE_2pnh|  PDB=2pnh  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRIB_ECOLI PRIB_ECOLI] Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.<ref>PMID:1856227</ref> <ref>PMID:1646811</ref> <ref>PMID:8366072</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pn/2pnh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pnh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Collapsed DNA replication forks must be reactivated through origin-independent reloading of the replication machinery (replisome) to ensure complete duplication of cellular genomes. In E. coli, the PriA-dependent pathway is the major replication restart mechanism and requires primosome proteins PriA, PriB, and DnaT for replisome reloading. However, the molecular mechanisms that regulate origin-independent replisome loading are not fully understood. Here, we demonstrate that assembly of primosome protein complexes represents a key regulatory mechanism, as inherently weak PriA-PriB and PriB-DnaT interactions are strongly stimulated by single-stranded DNA. Furthermore, the binding site on PriB for single-stranded DNA partially overlaps the binding sites for PriA and DnaT, suggesting a dynamic primosome assembly process in which single-stranded DNA is handed off from one primosome protein to another as a repaired replication fork is reactivated. This model helps explain how origin-independent initiation of DNA replication is restricted to repaired replication forks, preventing overreplication of the genome.
-===Escherichia coli PriB E39A variant===
+A hand-off mechanism for primosome assembly in replication restart.,Lopper M, Boonsombat R, Sandler SJ, Keck JL Mol Cell. 2007 Jun 22;26(6):781-93. PMID:17588514<ref>PMID:17588514</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_17588514}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2pnh" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 17588514 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17588514}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli K-12]]
-PNH is a 2 chains structure of sequences 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=2PNH OCA].
+[[Category: Large Structures]]
+[[Category: Keck JL]]
-==Reference==
+[[Category: Lopper ME]]
-<ref group="xtra">PMID:17588514</ref><references group="xtra"/>
-[[Category: Escherichia coli]]
-[[Category: Keck, J L.]]
-[[Category: Lopper, M E.]]
-[[Category: Beta barrel]]
-[[Category: Dna binding protein]]
-[[Category: Ob fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:21:42 2009''

2pnh

From Proteopedia

Current revision

Escherichia coli PriB E39A variant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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