Oganesyan Vaheh, Pufan Ramona, DeGiovanni Andrew, Yokota Hisao, Kim Rosalind, Kim Sung-Hou
Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1266-71. doi: 10.1107/S0907444904009394. Epub 2004 Jun 22.
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.
利用在硒峰波长处的反常衍射数据，通过X射线晶体学确定了化脓性链球菌推定的DNA结合蛋白SP_1288（gi/15675166，也列为gi/28895954）的晶体结构，分辨率为2.3埃。SP_1288属于一类蛋白质家族，其细胞功能与信号识别颗粒相关；到目前为止，关于该家族成员还没有结构信息。晶体学分析表明，SP_1288的整体折叠仅由α螺旋组成，并且该结构的75%与RNA聚合酶σ亚基的结构域4具有良好的相似性。这表明它可能参与转录起始的生化功能，其中包括与DNA的相互作用。
