Kostyuchenko Victor A, Leiman Petr G, Chipman Paul R, Kanamaru Shuji, van Raaij Mark J, Arisaka Fumio, Mesyanzhinov Vadim V, Rossmann Michael G
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 16/10 Miklukho-Maklaya Str., 117997 Moscow, Russia.
Nat Struct Biol. 2003 Sep;10(9):688-93. doi: 10.1038/nsb970. Epub 2003 Aug 17.
The baseplate of bacteriophage T4 is a multiprotein molecular machine that controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. We report here the three-dimensional structure of the baseplate-tail tube complex determined to a resolution of 12 A by cryoelectron microscopy. The baseplate has a six-fold symmetric, dome-like structure approximately 520 A in diameter and approximately 270 A long, assembled around a central hub. A 940 A-long and 96 A-diameter tail tube, coaxial with the hub, is connected to the top of the baseplate. At the center of the dome is a needle-like structure that was previously identified as a cell puncturing device. We have identified the locations of six proteins with known atomic structures, and established the position and shape of several other baseplate proteins. The baseplate structure suggests a mechanism of baseplate triggering and structural transition during the initial stages of T4 infection.
噬菌体T4的基板是一种多蛋白分子机器，可控制宿主细胞识别、附着、尾鞘收缩和病毒DNA喷射。我们在此报告通过冷冻电子显微镜确定的基板-尾管复合物的三维结构，分辨率为12埃。基板具有六重对称的圆顶状结构，直径约520埃，长约270埃，围绕着一个中心枢纽组装而成。一根与枢纽同轴的、长940埃、直径96埃的尾管连接到基板顶部。在圆顶中心是一个针状结构，以前被确定为细胞穿刺装置。我们已经确定了六种具有已知原子结构的蛋白质的位置，并确定了其他几种基板蛋白质的位置和形状。基板结构揭示了T4感染初始阶段基板触发和结构转变的机制。
