2MLG

Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx

Summary for 2MLG

• Entry DOI: 10.2210/pdb2mlg/pdb
• NMR Information: BMRB: 19821
• Descriptor: Sulfolobus transcription factor 76 aminoacid protein, Stf76 (1 entity in total)
• Functional Keywords: winged helix domain, dna binding protein
• Biological source: Fuselloviridae
• Total number of polymer chains: 1
• Total formula weight: 10306.95

Authors

Farina, B.,Russo, L.,Fattorusso, R. (deposition date: 2014-02-27, release date: 2014-03-12, Last modification date: 2024-05-01)

Primary citation

Contursi, P.,Farina, B.,Pirone, L.,Fusco, S.,Russo, L.,Bartolucci, S.,Fattorusso, R.,Pedone, E.
Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family.
Nucleic Acids Res., 42:5993-6011, 2014

PubMed Abstract: The hybrid plasmid-virus pSSVx from Sulfolobus islandicus presents an open reading frame encoding a 76 amino acid protein, namely Stf76, that does not show significant sequence homology with any protein with known 3D structure. The recombinant protein recognizes specifically two DNA-binding sites located in its own promoter, thus suggesting an auto-regulated role of its expression. Circular dichroism, spectrofluorimetric, light scattering and isothermal titration calorimetry experiments indicated a 2:1 molar ratio (protein:DNA) upon binding to the DNA target containing a single site. Furthermore, the solution structure of Stf76, determined by nuclear magnetic resonance (NMR) using chemical shift Rosetta software, has shown that the protein assumes a winged helix-turn-helix fold. NMR chemical shift perturbation analysis has been performed for the identification of the residues responsible for DNA interaction. In addition, a model of the Stf76-DNA complex has been built using as template a structurally related homolog.

PubMed: 24682827
DOI: 10.1093/nar/gku215

Experimental method

SOLUTION NMR