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Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.
Oganesyan, Vaheh; Pufan, Ramona; DeGiovanni, Andrew; Yokota, Hisao; Kim, Rosalind; Kim, Sung-Hou.
Afiliação
  • Oganesyan V; Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
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.
Assuntos
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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
Buscar no Google
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