Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.
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.
Oganesyan
Vaheh
V
Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Pufan
Ramona
R
DeGiovanni
Andrew
A
Yokota
Hisao
H
Kim
Rosalind
R
Kim
Sung-Hou
SH
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*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins