Cherney Maia M, Garen Craig R, James Michael N G
Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.
Biochim Biophys Acta. 2008 Nov;1784(11):1625-32. doi: 10.1016/j.bbapap.2008.05.012. Epub 2008 Jun 6.
We have determined the X-ray crystal structure of the Mycobacterium tuberculosis (Mtb) gene product encoded by the open reading frame Rv0760c at 1.50 A resolution by single-wavelength anomalous dispersion (SAD) phasing of diffraction data from crystals of the selenomethionine-substituted protein. Refinement against diffraction data from the native protein resulted in R(work)=19.5% and R(free)=21.4%. The X-ray crystal structure shows that the homodimeric Rv0760c polypeptide has an alpha + beta conical barrel fold placing it among many structural neighbors of the nuclear transport factor 2 family (NTF2). This family is highly conserved in terms of structure; however the substrates and individual protein functions are diverse. The structures of native Rv0760c in several different crystal forms and Rv0760c bound to 17beta-estradiol 17-hemisuccinate (EH) have also been solved and analyzed.
我们通过对硒代甲硫氨酸取代蛋白晶体的衍射数据进行单波长反常散射（SAD）相位分析，以1.50 Å的分辨率确定了结核分枝杆菌（Mtb）开放阅读框Rv0760c编码的基因产物的X射线晶体结构。根据天然蛋白的衍射数据进行精修，得到的R(work)=19.5%，R(free)=21.4%。X射线晶体结构表明，同二聚体Rv0760c多肽具有α + β锥形桶状折叠结构，使其与核转运因子2家族（NTF2）的许多结构相似物归为一类。该家族在结构上高度保守；然而，其底物和单个蛋白质功能却多种多样。我们还解析并分析了几种不同晶体形式的天然Rv0760c以及与17β-雌二醇17-半琥珀酸酯（EH）结合的Rv0760c的结构。
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