van Aalten D M, Knudsen J, DiRusso C C, Kokko T, Wierenga R K
Biocenter Oulu and Department of Biochemistry, University of Oulu, Linnanmaa, FIN-90570 Oulu, Finland.
Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):469-71. doi: 10.1107/s0907444900000937.
FadR, an acylCoA-dependent Escherichia coli transcription factor controlling the expression of genes involved in fatty-acid degradation and synthesis, has been crystallized. Crystals of two binary complexes were obtained. The FadR-CoA complex crystallized in space group C222(1), with unit-cell parameters a = 61.3, b = 102.0, c = 91.3 A. The FadR-octanoyl-CoA complex crystallized in space group P6(5)22, with unit-cell parameters a = b = 59.7, c = 296.2 A. Both crystal forms diffracted to 3.5 A on a rotating-anode generator. In both crystal forms, the asymmetric unit contains one subunit. The protein is known to be a homodimer; each subunit consists of two domains of unknown fold. For the acyl-CoA-binding domain, a previously undetected sequence homology to PAS domains, in particular the photoactive yellow protein, is reported.
FadR是一种依赖于酰基辅酶A的大肠杆菌转录因子，它控制着参与脂肪酸降解和合成的基因的表达，现已结晶。获得了两种二元复合物的晶体。FadR-辅酶A复合物在空间群C222(1)中结晶，晶胞参数为a = 61.3、b = 102.0、c = 91.3 Å。FadR-辛酰辅酶A复合物在空间群P6(5)22中结晶，晶胞参数为a = b = 59.7、c = 296.2 Å。两种晶体形式在旋转阳极发生器上的衍射分辨率均达到3.5 Å。在两种晶体形式中，不对称单元均包含一个亚基。已知该蛋白质为同型二聚体；每个亚基由两个折叠未知的结构域组成。对于酰基辅酶A结合结构域，报道了其与PAS结构域（特别是光活性黄色蛋白）之前未被检测到的序列同源性。
