4ou6

<StructureSection load='4ou6' size='340' side='right'caption='[[4ou6]], [[Resolution|resolution]] 1.96&Aring;' scene=''>

<table><tr><td colspan='2'>[[4ou6]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OU6 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ou7|4ou7]]</div></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=4ou6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ou6 OCA], [https://pdbe.org/4ou6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ou6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ou6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ou6 ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/DNAT_ECOLI DNAT_ECOLI]] This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'.[HAMAP-Rule:MF_01061]

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

DnaT is a primosomal protein that is required for the stalled replication fork restart in Escherichia coli. As an adapter, DnaT mediates the PriA-PriB-ssDNA ternary complex and the DnaB/C complex. However, the fundamental function of DnaT during PriA-dependent primosome assembly is still a black box. Here, we report the 2.83 A DnaT84-153-dT10 ssDNA complex structure, which reveals a novel three-helix bundle single-stranded DNA binding mode. Based on binding assays and negative-staining electron microscopy results, we found that DnaT can bind to phiX 174 ssDNA to form nucleoprotein filaments for the first time, which indicates that DnaT might function as a scaffold protein during the PriA-dependent primosome assembly. In combination with biochemical analysis, we propose a cooperative mechanism for the binding of DnaT to ssDNA and a possible model for the assembly of PriA-PriB-ssDNA-DnaT complex that sheds light on the function of DnaT during the primosome assembly and stalled replication fork restart. This report presents the first structure of the DnaT C-terminal complex with ssDNA and a novel model that explains the interactions between the three-helix bundle and ssDNA.

Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode.,Liu Z, Chen P, Wang X, Cai G, Niu L, Teng M, Li X Nucleic Acids Res. 2014 Jul 22. pii: gku633. PMID:25053836<ref>PMID:25053836</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 4ou6" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Chen, P]]

[[Category: Li, X]]

[[Category: Liu, Z]]

[[Category: Niu, L]]

[[Category: Teng, M]]

[[Category: Replication-dna complex]]