Publication Abstract from PubMed
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.
Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.,Oganesyan V, Pufan R, DeGiovanni A, Yokota H, Kim R, Kim SH Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1266-71. Epub 2004, Jun 22. PMID:15213388[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
