Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.
Acta Crystallogr D Biol Crystallogr
; 60(Pt 7): 1266-71, 2004 Jul.
Article
em En
| MEDLINE
| ID: mdl-15213388
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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Base de dados:
MEDLINE
Assunto principal:
Streptococcus pyogenes
/
Proteínas de Bactérias
/
Proteínas de Ligação a DNA
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article