title: Purification, crystallization and X-ray diffraction analysis of the C-terminal protease domain of Venezuelan equine encephalitis virus nsP2.
abstract: The C-terminal region of Venezuelan equine encephalitis virus (VEEV) nsP2 is responsible for proteolytic processing of the VEEV polyprotein replication complex. This action regulates the activity of the replication complex and is essential for viral replication, thus making nsP2 a very attractive target for development of VEEV therapeutics. The 338-amino-acid C-terminal region of VEEV nsP2 has been overexpressed in Escherichia coli, purified and crystallized. Crystals diffract to beyond 2.5 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1). Isomorphous heavy-atom derivatives suitable for phase analysis have been obtained and work on building a complete structural model is under way.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
authors.forename: Andrew T
authors.initials: AT
authors.lastname: Russo
authors.forename: Stanley J
authors.initials: SJ
authors.lastname: Watowich
mesh_terms: D003460:Crystallization; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D004685:Encephalomyelitis, Venezuelan Equine / Q000201:enzymology*; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D014764:Viral Proteins; D003546:Cysteine Endopeptidases; C078306:nsP2 proteinase