1S7O

Crystal structure of putative DNA binding protein SP_1288 from Streptococcus pygenes

Summary for 1S7O

• Entry DOI: 10.2210/pdb1s7o/pdb
• Descriptor: Hypothetical UPF0122 protein SPy1201/SpyM3_0842/SPs1042/spyM18_1152 (2 entities in total)
• Functional Keywords: putative dna binding protein; structural genomics, signal recognition particle, rna polymerase sigma factor, x-rat crystallography, upf0122, structure funded by nih, psi, protein structure initiative, berkeley structural genomics center, bsgc, structural genomics, unknown function
• Biological source: Streptococcus pyogenes serotype M3
• Total number of polymer chains: 3
• Total formula weight: 40812.88

Authors

Oganesyan, V.,Pufan, R.,DeGiovanni, A.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2004-01-29, release date: 2004-06-29, Last modification date: 2024-02-14)

Primary citation

Oganesyan, V.,Pufan, R.,DeGiovanni, A.,Yokota, H.,Kim, R.,Kim, S.H.
Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes.
Acta Crystallogr.,Sect.D, 60:1266-1271, 2004

PubMed 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.

PubMed: 15213388
DOI: 10.1107/S0907444904009394

Experimental method

X-RAY DIFFRACTION (2.31 Å)