Crystallization and preliminary X-ray diffraction analysis of central structure domains from mumps virus F protein.
Fusion of members of the Paramyxoviridae family involves two glycoproteins: the attachment protein and the fusion protein. Changes in the fusion-protein conformation were caused by binding of the attachment protein to the cellular receptor. In the membrane-fusion process, two highly conserved heptad-repeat (HR) regions, HR1 and HR2, are believed to form a stable six-helix coiled-coil bundle. However, no crystal structure has yet been determined for this state in the mumps virus (MuV, a member of the Paramyxoviridae family). In this study, a single-chain protein consisting of two HR regions connected by a flexible amino-acid linker (named 2-Helix) was expressed, purified and crystallized by the hanging-drop vapour-diffusion method. A complete X-ray data set was obtained in-house to 2.2 A resolution from a single crystal. The crystal belongs to space group C2, with unit-cell parameters a = 161.2, b = 60.8, c = 40.1 A, beta = 98.4 degrees. The crystal structure will help in understanding the molecular mechanism of Paramyxoviridae family membrane fusion.
Liu
Yueyong
Y
Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
Xu
Yanhui
Y
Zhu
Jieqing
J
Qiu
Bingsheng
B
Rao
Zihe
Z
Gao
George F
GF
Tien
Po
P
D003460:Crystallization; D009109:Mumps virus / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
D014764:Viral Proteins