Crystal structure of vesicular stomatitis virus matrix protein
Crystal structure of vesicular stomatitis virus matrix protein
复制标题
DOI：
10.1093/emboj/cdf284
复制
发表时间：
2002-06-17
期刊：
影响因子：
11.4
通讯作者：
Knossow, M
中科院分区：
文献类型：
--
作者：
Gaudier, M;Gaudin, Y;Knossow, M
水泡性口炎病毒 (VSV) 基质蛋白 (M) 与细胞膜相互作用、自缔合，并在病毒组装和出芽中发挥重要作用。我们展示了 VSV M 的可溶性嗜热菌蛋白酶抗性核心的晶体结构，以 1.96 埃分辨率确定。该折叠是其他水泡病毒基质蛋白共享的新折叠。该结构解释了出芽缺陷的 M 温度敏感突变体稳定性丧失的原因，并揭示了从球状核心突出的柔性环，这对于自组装非常重要。膜漂浮表明，该蛋白的第二个结构域与富含 M 赖氨酸的 N 端肽一起参与膜结合。事实上，该结构揭示了靠近疏水环的疏水表面，并被可能构成该结构域的保守碱性残基包围。最后，负链病毒基质蛋白与逆转录病毒 Gag 蛋白的比较表明，它们的主要膜结合域和其余结构之间的灵活连接是这些参与出芽和病毒组装的蛋白质共有的共同特征。
The vesicular stomatitis virus (VSV) matrix protein (M) interacts with cellular membranes, self-associates and plays a major role in virus assembly and budding. We present the crystallographic structure, determined at 1.96 Angstrom resolution, of a soluble thermolysin resistant core of VSV M. The fold is a new fold shared by the other vesiculovirus matrix proteins. The structure accounts for the loss of stability of M temperature-sensitive mutants deficient in budding, and reveals a flexible loop protruding from the globular core that is important for self-assembly. Membrane floatation shows that, together with the M lysine-rich N-terminal peptide, a second domain of the protein is involved in membrane binding. Indeed, the structure reveals a hydrophobic surface located close to the hydrophobic loop and surrounded by conserved basic residues that may constitute this domain. Lastly, comparison of the negative-stranded virus matrix proteins with retrovirus Gag proteins suggests that the flexible link between their major membrane binding domain and the rest of the structure is a common feature shared by these proteins involved in budding and virus assembly.