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7BBQ

Crystal structure of the HTH DNA binding protein ArdK from R388 plasmid. Apo form.

Summary for 7BBQ
Entry DOI10.2210/pdb7bbq/pdb
DescriptorKORA domain-containing protein (1 entity in total)
Functional Keywordsdna binding protein, helix turn helix, direct repeat, plasmid conjugation
Biological sourceEscherichia coli K-12
Total number of polymer chains1
Total formula weight12658.80
Authors
Fernandez-Lopez, R.,Boer, D.R.,Moncalian, G. (deposition date: 2020-12-18, release date: 2022-07-13, Last modification date: 2024-10-23)
Primary citationFernandez-Lopez, R.,Ruiz, R.,Del Campo, I.,Gonzalez-Montes, L.,Boer, D.R.,de la Cruz, F.,Moncalian, G.
Structural basis of direct and inverted DNA sequence repeat recognition by helix-turn-helix transcription factors.
Nucleic Acids Res., 50:11938-11947, 2022
Cited by
PubMed Abstract: Some transcription factors bind DNA motifs containing direct or inverted sequence repeats. Preference for each of these DNA topologies is dictated by structural constraints. Most prokaryotic regulators form symmetric oligomers, which require operators with a dyad structure. Binding to direct repeats requires breaking the internal symmetry, a property restricted to a few regulators, most of them from the AraC family. The KorA family of transcriptional repressors, involved in plasmid propagation and stability, includes members that form symmetric dimers and recognize inverted repeats. Our structural analyses show that ArdK, a member of this family, can form a symmetric dimer similar to that observed for KorA, yet it binds direct sequence repeats as a non-symmetric dimer. This is possible by the 180° rotation of one of the helix-turn-helix domains. We then probed and confirmed that ArdK shows affinity for an inverted repeat, which, surprisingly, is also recognized by a non-symmetrical dimer. Our results indicate that structural flexibility at different positions in the dimerization interface constrains transcription factors to bind DNA sequences with one of these two alternative DNA topologies.
PubMed: 36370103
DOI: 10.1093/nar/gkac1024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

239149

數據於2025-07-23公開中

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