6aeq: Difference between revisions
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==Crystal structure of the ssDNA-binding domain of DnaT from Salmonella enterica Serovar Typhimurium LT2== | |||
<StructureSection load='6aeq' size='340' side='right'caption='[[6aeq]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6aeq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEQ 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=6aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aeq OCA], [http://pdbe.org/6aeq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aeq RCSB], [http://www.ebi.ac.uk/pdbsum/6aeq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aeq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/DNAT_SALTY DNAT_SALTY]] 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'. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DnaT is a replication restart primosomal protein required for re-initiating chromosomal DNA replication in bacteria. DnaT can be a monomer, dimer, trimer, tetramer, or pentamer. The oligomerization and disassembly of DnaT oligomers are critical in primosome assembly. Prior to this work, only the ssDNA-bound structure of the pentameric DnaT truncated protein (aa 84-153; DnaT84-153) was available. The mechanism by which DnaT oligomerizes as different states is unclear. In this paper, we report the crystal structure of the C-terminal domain of DnaT (aa 84-179; DnaTc) at 2.30A resolution (PDB entry 6AEQ). DnaTc forms a dimer both in the crystalline state and in solution. As compared with the ssDNA-bound structure of the pentameric DnaT84-153, their subunit-subunit interfaces significantly differ. The different oligomeric architecture suggests a strong conformational change possibly induced by ssDNA. Superposition analysis further indicated that the monomer of a DnaTc dimer shifted away by a distance of 7.5A and rotated by an angle of 170 degrees for binding to ssDNA. Basing from these molecular evidence, we discussed and proposed a working model to explain how DnaTc oligomerizes through residue R146 mediation. | |||
Crystal structure of the C-terminal domain of the primosomal DnaT protein: Insights into a new oligomerization mechanism.,Chen KL, Huang YH, Liao JF, Lee WC, Huang CY Biochem Biophys Res Commun. 2019 Mar 26;511(1):1-6. doi:, 10.1016/j.bbrc.2019.02.026. Epub 2019 Feb 10. PMID:30755302<ref>PMID:30755302</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Huang, C | <div class="pdbe-citations 6aeq" style="background-color:#fffaf0;"></div> | ||
[[Category: Huang, Y | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Huang, C Y]] | |||
[[Category: Huang, Y H]] | |||
[[Category: Dna binding]] | |||
[[Category: Dna binding protein]] | |||
[[Category: Dnat]] | |||
[[Category: Primosome]] | |||
[[Category: Replication restart]] | |||
