6aeq

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Crystal structure of the ssDNA-binding domain of DnaT from Salmonella enterica Serovar Typhimurium LT2

Structural highlights

6aeq is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2518084Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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'.

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^[1]

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

References

↑ Chen KL, Huang YH, Liao JF, Lee WC, Huang CY. Crystal structure of the C-terminal domain of the primosomal DnaT protein: Insights into a new oligomerization mechanism. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2019.02.026