7bbq
From Proteopedia
Crystal structure of the HTH DNA binding protein ArdK from R388 plasmid. Apo form.
Structural highlights
FunctionPublication Abstract from PubMedSome 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 degrees 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. Structural basis of direct and inverted DNA sequence repeat recognition by helix-turn-helix transcription factors.,Fernandez-Lopez R, Ruiz R, Del Campo I, Gonzalez-Montes L, Boer DR, de la Cruz F, Moncalian G Nucleic Acids Res. 2022 Nov 11;50(20):11938-11947. doi: 10.1093/nar/gkac1024. PMID:36370103[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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