Spahn C M, Blaha G, Agrawal R K, Penczek P, Grassucci R A, Trieber C A, Connell S R, Taylor D E, Nierhaus K H, Frank J
Howard Hughes Medical Institute, Health Research Inc. at the Wadsworth Center, Empire State Plaza, Albany, NY 12201, USA.
Mol Cell. 2001 May;7(5):1037-45. doi: 10.1016/s1097-2765(01)00238-6.
Tet(O) belongs to a class of ribosomal protection proteins that mediate tetracycline resistance. It is a G protein that shows significant sequence similarity to elongation factor EF-G. Here we present a cryo-electron microscopic reconstruction, at 16 A resolution, of its complex with the E. coli 70S ribosome. Tet(O) was bound in the presence of a noncleavable GTP analog to programmed ribosomal complexes carrying fMet-tRNA in the P site. Tet(O) is directly visible as a mass close to the A-site region, similar in shape and binding position to EF-G. However, there are important differences. One of them is the different location of the tip of domain IV, which in the Tet(O) case, does not overlap with the ribosomal A site but is directly adjacent to the primary tetracycline binding site. Our findings give insights into the mechanism of tetracycline resistance.
Tet(O)属于一类介导四环素抗性的核糖体保护蛋白。它是一种G蛋白,与延伸因子EF-G具有显著的序列相似性。在此,我们展示了其与大肠杆菌70S核糖体复合物在16埃分辨率下的冷冻电子显微镜重建结果。Tet(O)在不可切割的GTP类似物存在的情况下,与在P位点携带fMet-tRNA的程序化核糖体复合物结合。Tet(O)作为靠近A位点区域的一个团块直接可见,其形状和结合位置与EF-G相似。然而,存在重要差异。其中之一是结构域IV尖端的不同位置,在Tet(O)的情况下,它不与核糖体A位点重叠,而是直接邻近主要的四环素结合位点。我们的发现为四环素抗性机制提供了见解。