5wtn

<StructureSection load='5wtn' size='340' side='right' caption='[[5wtn]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[5wtn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WTN FirstGlance]. <br>

</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=5wtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wtn OCA], [http://pdbe.org/5wtn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wtn RCSB], [http://www.ebi.ac.uk/pdbsum/5wtn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wtn ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The DnaB primosomal protein from Gram-positive bacteria plays a key role in DNA replication and restart as a loader protein for the recruitment of replisome cascade proteins. Previous investigations have established that DnaB is composed of an N-terminal domain, a middle domain, and a C-terminal domain. However, structural evidence for how DnaB functions at the atomic level is lacking. Here, we report the crystal structure of DnaB, encompassing the N-terminal and middle domains (residues 1-300), from Geobacillus stearothermophilus (GstDnaB1-300) at 2.8 A resolution. Our structure revealed that GstDnaB1-300 forms a tetramer with two basket-like architecture, a finding s consistent with those from solution studies using analytical ultracentrifugation. Furthermore, our results from both GST pull-down assays and analytical ultracentrifugation show that GstDnaB1-300 is sufficient to form a complex with PriA, the primosomal re-initiation protein. Moreover, with the aid of small angle X-ray scattering (SAXS) experiments, we also determined the structural envelope of full-length DnaB (GstDnaBFL) in solution. These SAXS studies indicated that GstDnaBFL has an elongated conformation and that the protruding density envelopes originating from GstDnaB1-300 could completely accommodate the GstDnaB C-terminal domain (residues 301-461) . Taken together with biochemical assays, our results suggest that GstDnaB uses different domains to distinguish the PriA-interaction and ssDNA-binding. This finding can further extend our understanding of primosomal assembly in replication restart.

Structural analyses of the bacterial primosomal protein DnaB reveal that it is a tetramer and forms a complex with a primosomal re-initiation protein.,Li YC, Naveen V, Lin MG, Hsiao CD J Biol Chem. 2017 Aug 14. pii: jbc.M117.792002. doi: 10.1074/jbc.M117.792002. PMID:28808061<ref>PMID:28808061</ref>

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

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<div class="pdbe-citations 5wtn" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hsiao, C D]]

[[Category: Li, Y C]]

[[Category: Dna replication]]

[[Category: Dnab]]

[[Category: Replication]]