Crystallization and preliminary X-ray analysis of the C-terminal cytoplasmic domain of FlhA, a membrane-protein subunit of the bacterial flagellar type III protein-export apparatus
- Dynamic NanoMachine Project, ICORP, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871 (Japan)
- Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114 (United States)
Crystals of the cytoplasmic domain of FlhA, a membrane-protein component of the bacterial flagellar type III protein-export apparatus from Salmonella, have been obtained and characterized by X-ray diffraction. The axial components of the bacterial flagellum and the scaffolding proteins for its assembly are exported through the flagellar-specific type III protein-export apparatus, which is believed to be located on the cytoplasmic surface of the basal body. FlhA is an essential component of the type III export apparatus of Salmonella and consists of two major portions: an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhA{sub C}). FlhA{sub C} and a 38 kDa fragment of FlhA{sub C} (FlhA{sub C}38K) were purified and crystallized. The crystals were obtained by the sitting-drop vapour-diffusion technique with PEG 8000 as a precipitant. FlhA{sub C} crystals grew in the tetragonal space group I4{sub 1}/I4{sub 3}, with unit-cell parameters a = b = 216.6, c = 65.0 Å. FlhA{sub C}38K was crystallized in an orthorhombic form, with unit-cell parameters a = 53.0, b = 93.1, c = 186.5 Å. X-ray diffraction data from crystals of FlhA{sub C} and the SeMet derivative of FlhA{sub C} were collected to 2.9 and 3.2 Å, respectively.
- OSTI ID:
- 22356032
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 6; Other Information: PMCID: PMC1952338; PMID: 16511106; PUBLISHER-ID: fw5034; OAI: oai:pubmedcentral.nih.gov:1952338; 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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