Crystallization and preliminary X-ray diffraction analysis of central structure domains from mumps virus F protein
- Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080 (China)
- Laboratory of Structural Biology and MOE Laboratory of Protein Sciences, School of Life Sciences and Bioengineering, Tsinghua University, Beijing 100084 (China)
Single crystals of the central structure domains from mumps virus F protein have been obtained by the hanging-drop vapour-diffusion method. A diffraction data set has been collected to 2.2 Å resolution. 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 C2, 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.
- OSTI ID:
- 22356164
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 9; Other Information: PMCID: PMC1978114; PMID: 16511178; PUBLISHER-ID: vr5043; OAI: oai:pubmedcentral.nih.gov:1978114; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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