1S7O

Crystal structure of putative DNA binding protein SP_1288 from Streptococcus pygenes

1S7O の概要

• エントリーDOI: 10.2210/pdb1s7o/pdb
• 分子名称: Hypothetical UPF0122 protein SPy1201/SpyM3_0842/SPs1042/spyM18_1152 (2 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Streptococcus pyogenes serotype M3
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40812.88

構造登録者

Oganesyan, V.,Pufan, R.,DeGiovanni, A.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (登録日: 2004-01-29, 公開日: 2004-06-29, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.31 Å)