Khamrui Susmita, Ranjan Amitabh, Pani Bibhusita, Sen Ranjan, Sen Udayaditya
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhan Nagar, Kolkata 700 064, India.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):204-6. doi: 10.1107/S1744309109053846. Epub 2010 Jan 28.
Psu, a coat protein from bacteriophage P4, inhibits Rho-dependent transcription termination both in vivo and in vitro. The Psu protein is alpha-helical in nature and appeared to be a dimer in solution. It interacts with Rho and affects the ATP binding and RNA-dependent ATPase activity of Rho, which in turn reduces the rate of RNA release from the elongation complex. Crystals of Psu were grown in space group I422 in the presence of PEG, with unit-cell parameters a = b = 148.76, c = 63.38 A and a calculated Matthews coefficient of 2.1 A(3) Da(-1) (41.5% solvent content), assuming the presence of two molecules in the asymmetric unit. A native data set was collected to 2.3 A resolution.
噬菌体P4的外壳蛋白Psu在体内和体外均抑制Rho依赖性转录终止。Psu蛋白本质上是α螺旋结构，在溶液中似乎以二聚体形式存在。它与Rho相互作用，影响Rho的ATP结合和RNA依赖性ATPase活性，进而降低RNA从延伸复合物中释放的速率。Psu晶体在存在聚乙二醇（PEG）的情况下于空间群I422中生长，晶胞参数a = b = 148.76，c = 63.38 Å，假设不对称单元中存在两个分子，计算得到的马修斯系数为2.1 ų Da⁻¹（溶剂含量41.5%）。收集到了分辨率为2.3 Å的天然数据集。
