View source for 2ncj


==Solution Structure of the PriC DNA replication restart protein==
<StructureSection load='2ncj' size='340' side='right'caption='[[2ncj]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ncj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cronobacter_sakazakii_ATCC_BAA-894 Cronobacter sakazakii ATCC BAA-894]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NCJ 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=2ncj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ncj OCA], [https://pdbe.org/2ncj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ncj RCSB], [https://www.ebi.ac.uk/pdbsum/2ncj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ncj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A7MJV9_CROS8 A7MJV9_CROS8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CCollisions between DNA replication complexes (replisomes) and barriers such as damaged DNA or tightly bound protein complexes can dissociate replisomes from chromosomes prematurely. Replisomes must be reloaded under these circumstances to avoid incomplete replication and cell death. Bacteria have evolved multiple pathways that initiate DNA replication restart by recognizing and remodeling abandoned replication forks and reloading the replicative helicase. In vitro, the simplest of these pathways is mediated by the single-domain PriC protein, which, along with the DnaC helicase loader, can load the DnaB replicative helicase onto DNA bound by the single-stranded (ss) DNA binding protein (SSB). Previous biochemical studies have identified PriC residues that mediate interactions with ssDNA and SSB. However, the mechanisms by which PriC drives DNA replication restart have remained poorly defined due to the limited structural information available for PriC. Here, we report the NMR structure of full-length PriC from Cronobacter sakazakii. PriC forms a compact bundle of alpha helices that brings together residues involved in ssDNA and SSB binding at adjacent sites on the protein surface. Disruption of these interaction sites and of other conserved residues leads to decreased DnaB helicase loading onto SSB-bound DNA. We also demonstrate that PriC can directly interact with DnaB and the DnaB/DnaC complex. These data lead to a model in which PriC acts as a scaffold for recruiting DnaB/DnaC to SSB/ssDNA sites present at stalled replication forks.

Structure and Function of the PriC DNA Replication Restart Protein.,Wessel SR, Cornilescu CC, Cornilescu G, Metz A, Leroux M, Hu K, Sandler SJ, Markley JL, Keck JL J Biol Chem. 2016 Jul 5. pii: jbc.M116.738781. PMID:27382050<ref>PMID:27382050</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ncj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Cronobacter sakazakii ATCC BAA-894]]
[[Category: Large Structures]]
[[Category: Cornilescu CC]]
[[Category: Cornilescu G]]
[[Category: Keck JL]]
[[Category: Markley JL]]
[[Category: Wessel SR]]