Structural highlights
Function
[Y1201_STRP1] Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Oganesyan V, Pufan R, DeGiovanni A, Yokota H, Kim R, Kim SH. Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes. Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1266-71. Epub 2004, Jun 22. PMID:15213388 doi:10.1107/S0907444904009394
