Lakshminarasimhan Damodharan, Eswaramoorthy Subramaniam, Burley Stephen K, Swaminathan Subramanyam
Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):8-11. doi: 10.1107/S1744309109047009. Epub 2009 Dec 25.
The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 A, beta = 113.4 degrees , and contained three protein molecules in the asymmetric unit. The structure was determined by the single-wavelength anomalous dispersion method using selenium-labeled protein and was refined to a final R factor of 24.7% (R(free) = 28.0%). The protein molecule mainly comprises a three-helical bundle. Its putative function is inferred to be single-stranded nucleic acid binding based on sequence and structural homology.
已确定来自枯草芽孢杆菌的假设蛋白YqgQ的晶体结构,分辨率为2.1埃。晶体属于空间群P2(1),晶胞参数a = 51.85、b = 41.25、c = 55.18埃,β = 113.4°,不对称单位中包含三个蛋白质分子。通过使用硒标记蛋白的单波长反常色散法确定了结构,并将其精修至最终R因子为24.7%(R(free)=28.0%)。该蛋白质分子主要由一个三螺旋束组成。基于序列和结构同源性,推测其假定功能为单链核酸结合。