title: Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.
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.
authors.affiliation: Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
authors.forename: Vaheh
authors.initials: V
authors.lastname: Oganesyan
authors.forename: Ramona
authors.initials: R
authors.lastname: Pufan
authors.forename: Andrew
authors.initials: A
authors.lastname: DeGiovanni
authors.forename: Hisao
authors.initials: H
authors.lastname: Yokota
authors.forename: Rosalind
authors.initials: R
authors.lastname: Kim
authors.forename: Sung-Hou
authors.initials: SH
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D016415:Sequence Alignment; D013297:Streptococcus pyogenes / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins