7TZ1
Crystal Structure of a Mycobacteriophage Cluster A2 Immunity Repressor:DNA Complex
Summary for 7TZ1
Entry DOI | 10.2210/pdb7tz1/pdb |
Related | 7R6R |
Descriptor | Immunity repressor, DNA (5'-D(P*TP*TP*TP*CP*GP*GP*TP*GP*GP*CP*TP*GP*TP*CP*AP*AP*GP*CP*GP*GP*G)-3'), DNA (5'-D(P*CP*CP*CP*GP*CP*TP*TP*GP*AP*CP*AP*GP*CP*CP*AP*CP*CP*GP*AP*AP*A)-3') (3 entities in total) |
Functional Keywords | immunity repressor, helix-turn-helix motif, dna binding protein, gene regulation, gene regulation-dna complex, gene regulation/dna |
Biological source | Mycobacterium phage TipsytheTRex More |
Total number of polymer chains | 3 |
Total formula weight | 36812.38 |
Authors | McGinnis, R.J.,Brambley, C.A.,Stamey, B.,Green, W.C.,Gragg, K.N.,Cafferty, E.R.,Terwilliger, T.C.,Hammel, M.,Hollis, T.J.,Miller, J.M.,Gainey, M.D.,Wallen, J.R. (deposition date: 2022-02-15, release date: 2022-07-20, Last modification date: 2024-10-23) |
Primary citation | McGinnis, R.J.,Brambley, C.A.,Stamey, B.,Green, W.C.,Gragg, K.N.,Cafferty, E.R.,Terwilliger, T.C.,Hammel, M.,Hollis, T.J.,Miller, J.M.,Gainey, M.D.,Wallen, J.R. A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence. Nat Commun, 13:4105-4105, 2022 Cited by PubMed Abstract: Regulation of bacteriophage gene expression involves repressor proteins that bind and downregulate early lytic promoters. A large group of mycobacteriophages code for repressors that are unusual in also terminating transcription elongation at numerous binding sites (stoperators) distributed across the phage genome. Here we provide the X-ray crystal structure of a mycobacteriophage immunity repressor bound to DNA, which reveals the binding of a monomer to an asymmetric DNA sequence using two independent DNA binding domains. The structure is supported by small-angle X-ray scattering, DNA binding, molecular dynamics, and in vivo immunity assays. We propose a model for how dual DNA binding domains facilitate regulation of both transcription initiation and elongation, while enabling evolution of other superinfection immune specificities. PubMed: 35835745DOI: 10.1038/s41467-022-31678-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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