title: Crystallization and preliminary X-ray diffraction analysis of central structure domains from mumps virus F protein.
abstract: 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.
authors.affiliation: Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
authors.forename: Yueyong
authors.initials: Y
authors.lastname: Liu
authors.forename: Yanhui
authors.initials: Y
authors.lastname: Xu
authors.forename: Jieqing
authors.initials: J
authors.lastname: Zhu
authors.forename: Bingsheng
authors.initials: B
authors.lastname: Qiu
authors.forename: Zihe
authors.initials: Z
authors.lastname: Rao
authors.forename: George F
authors.initials: GF
authors.lastname: Gao
authors.forename: Po
authors.initials: P
authors.lastname: Tien
mesh_terms: D003460:Crystallization; D009109:Mumps virus / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D014764:Viral Proteins