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7TZV

Structure of DriD C-domain bound to 9mer ssDNA

Summary for 7TZV
Entry DOI10.2210/pdb7tzv/pdb
DescriptorWYL domain-containing protein, DNA (5'-D(*TP*AP*GP*TP*CP*TP*AP*CP*T)-3') (3 entities in total)
Functional Keywordsdrid, dna repair, sos-independent, wyl domain, whth, transcription
Biological sourceCaulobacter vibrioides
More
Total number of polymer chains3
Total formula weight46771.78
Authors
Schumacher, M.A.,Laub, M. (deposition date: 2022-02-16, release date: 2022-06-01, Last modification date: 2024-04-03)
Primary citationGozzi, K.,Salinas, R.,Nguyen, V.D.,Laub, M.T.,Schumacher, M.A.
ssDNA is an allosteric regulator of the C. crescentus SOS-independent DNA damage response transcription activator, DriD.
Genes Dev., 36:618-633, 2022
Cited by
PubMed Abstract: DNA damage repair systems are critical for genomic integrity. However, they must be coordinated with DNA replication and cell division to ensure accurate genomic transmission. In most bacteria, this coordination is mediated by the SOS response through LexA, which triggers a halt in cell division until repair is completed. Recently, an SOS-independent damage response system was revealed in This pathway is controlled by the transcription activator, DriD, but how DriD senses and signals DNA damage is unknown. To address this question, we performed biochemical, cellular, and structural studies. We show that DriD binds a specific promoter DNA site via its N-terminal HTH domain to activate transcription of genes, including the cell division inhibitor A structure of the C-terminal portion of DriD revealed a WYL motif domain linked to a WCX dimerization domain. Strikingly, we found that DriD binds ssDNA between the WYL and WCX domains. Comparison of apo and ssDNA-bound DriD structures reveals that ssDNA binding orders and orients the DriD domains, indicating a mechanism for ssDNA-mediated operator DNA binding activation. Biochemical and in vivo studies support the structural model. Our data thus reveal the molecular mechanism underpinning an SOS-independent DNA damage repair pathway.
PubMed: 35618312
DOI: 10.1101/gad.349541.122
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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