Crystallization and preliminary X-ray diffraction analysis of central structure domains from mumps virus F protein. Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 Sep 01;61(Pt 9):855-7
Date
03/03/2006Pubmed ID
16511178Pubmed Central ID
PMC1978114DOI
10.1107/S1744309105025789Scopus ID
2-s2.0-33747050666 (requires institutional sign-in at Scopus site) 4 CitationsAbstract
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.
Author List
Liu Y, Xu Y, Zhu J, Qiu B, Rao Z, Gao GF, Tien PAuthor
Jieqing Zhu PhD Assistant Professor, Associate Investigator in the Biochemistry department at BloodCenter of WisconsinMESH terms used to index this publication - Major topics in bold
CrystallizationMumps virus
Protein Structure, Tertiary
Viral Proteins
X-Ray Diffraction