2KEL
Structure of the transcription regulator SvtR from the hyperthermophilic archaeal virus SIRV1
Summary for 2KEL
| Entry DOI | 10.2210/pdb2kel/pdb |
| NMR Information | BMRB: 16153 |
| Descriptor | Uncharacterized protein 56B (1 entity in total) |
| Functional Keywords | protein, homodimer, ribbon-helix-helix, transcription repressor |
| Biological source | Sulfolobus islandicus rod-shaped virus 1 (SIRV-1) |
| Total number of polymer chains | 2 |
| Total formula weight | 13265.45 |
| Authors | Guilliere, F.,Kessler, A.,Peixeiro, N.,Sezonov, G.,Prangishvili, D.,Delepierre, M.,Guijarro, J.I. (deposition date: 2009-01-30, release date: 2009-06-16, Last modification date: 2024-05-22) |
| Primary citation | Guilliere, F.,Peixeiro, N.,Kessler, A.,Raynal, B.,Desnoues, N.,Keller, J.,Delepierre, M.,Prangishvili, D.,Sezonov, G.,Guijarro, J.I. Structure, function, and targets of the transcriptional regulator SvtR from the hyperthermophilic archaeal virus SIRV1. J.Biol.Chem., 284:22222-22237, 2009 Cited by PubMed Abstract: We have characterized the structure and the function of the 6.6-kDa protein SvtR (formerly called gp08) from the rod-shaped virus SIRV1, which infects the hyperthermophilic archaeon Sulfolobus islandicus that thrives at 85 degrees C in hot acidic springs. The protein forms a dimer in solution. The NMR solution structure of the protein consists of a ribbon-helix-helix (RHH) fold between residues 13 and 56 and a disordered N-terminal region (residues 1-12). The structure is very similar to that of bacterial RHH proteins despite the low sequence similarity. We demonstrated that the protein binds DNA and uses its beta-sheet face for the interaction like bacterial RHH proteins. To detect all the binding sites on the 32.3-kb SIRV1 linear genome, we designed and performed a global genome-wide search of targets based on a simplified electrophoretic mobility shift assay. Four targets were recognized by the protein. The strongest binding was observed with the promoter of the gene coding for a virion structural protein. When assayed in a host reconstituted in vitro transcription system, the protein SvtR (Sulfolobus virus transcription regulator) repressed transcription from the latter promoter, as well as from the promoter of its own gene. PubMed: 19535331DOI: 10.1074/jbc.M109.029850 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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