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  • Title: Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.
    Author: Oganesyan V, Pufan R, DeGiovanni A, Yokota H, Kim R, Kim SH.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 Jul; 60(Pt 7):1266-71. PubMed ID: 15213388.
    Abstract:
    The crystal structure of the putative DNA-binding protein SP_1288 (gi/15675166, also listed as gi/28895954) from Streptococcus pyogenes has been determined by X-ray crystallography to a resolution of 2.3 A using anomalous diffraction data at the Se peak wavelength. SP_1288 belongs to a family of proteins whose cellular function is associated with the signal recognition particle; no structural information has been available until now about the members of the family. Crystallographic analysis revealed that the overall fold of SP_1288 consists exclusively of alpha-helices and that 75% of the structure has good similarity to domain 4 of the sigma subunit of RNA polymerase. This suggests its possible involvement in the biochemical function of transcription initiation, which includes interaction with DNA.
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