Open AccessCrystallization and preliminary X‐ray diffraction analysis of central structure domains from mumps virus F protein
Author(s) -
Liu Yueyong,
Xu Yanhui,
Zhu Jieqing,
Qiu Bingsheng,
Rao Zihe,
Gao George F.,
Tien Po
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105025789
Subject(s) - heptad repeat , paramyxoviridae , crystallography , lipid bilayer fusion , mumps virus , protein structure , viral protein , peptide sequence , protein folding , fusion protein , chemistry , biology , biophysics , virus , virology , biochemistry , recombinant dna , viral disease , gene
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 Å resolution from a single crystal. The crystal belongs to space group C 2, with unit‐cell parameters a = 161.2, b = 60.8, c = 40.1 Å, β = 98.4°. The crystal structure will help in understanding the molecular mechanism of Paramyxoviridae family membrane fusion.