Crowther R A, Kiselev N A, Böttcher B, Berriman J A, Borisova G P, Ose V, Pumpens P
Medical Research Council, Laboratory of Molecular Biology, Cambridge, England.
Cell. 1994 Jun 17;77(6):943-50. doi: 10.1016/0092-8674(94)90142-2.
Human hepatitis B virus core protein expressed in E. coli assembles into two sizes of particle. We have determined their three-dimensional structures by electron cryomicroscopy and image processing. The large and small particles correspond to triangulation number T = 4 and T = 3 dimer clustered packings, containing 240 and 180 protein subunits, respectively. The local packing of subunits is very similar in the two sizes of particle and shows holes or channels through the shell. The native viral core particle packages RNA and is active in reverse transcription to DNA. The holes we observe may provide access for the necessary small molecules. Shells assembled from the intact core protein contain additional material, probably RNA, which appears as an icosahedrally ordered inner shell in the three-dimensional map.
在大肠杆菌中表达的人乙肝病毒核心蛋白组装成两种大小的颗粒。我们通过电子冷冻显微镜和图像处理确定了它们的三维结构。大颗粒和小颗粒分别对应于三角剖分数T = 4和T = 3的二聚体聚集堆积，分别包含240和180个蛋白质亚基。两种大小颗粒中亚基的局部堆积非常相似，并显示出贯穿外壳的孔或通道。天然病毒核心颗粒包裹RNA并在逆转录成DNA过程中具有活性。我们观察到的孔可能为必需的小分子提供通道。由完整核心蛋白组装的外壳包含额外的物质，可能是RNA，在三维图谱中表现为二十面体有序的内壳。
