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T. Minamino, R. Macnab (1999)
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Y. Saijo-Hamano, T. Minamino, R. Macnab, K. Namba (2004)
Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella.Journal of molecular biology, 343 2
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Keng Zhu, B. González-Pedrajo, R. Macnab (2002)
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(1992)
Jnt CCP 4 / ESF – EACBM Newsl
(2003)
Mol
T. Minamino, R. Macnab (2000)
Interactions among components of the Salmonella flagellar export apparatus and its substratesMolecular Microbiology, 35
G. Dreyfus, Andrew Williams, I. Kawagishi, R. Macnab, M. Homma, V. Irikura, M. R., Macnab, J. Buysse (1993)
Genetic and biochemical analysis of Salmonella typhimurium FliI, a flagellar protein related to the catalytic subunit of the F0F1 ATPase and to virulence proteins of mammalian and plant pathogensJournal of Bacteriology, 175
T. Minamino, R. Macnab (2000)
FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activityMolecular Microbiology, 37
F. Auvray, A. Ozin, L. Claret, C. Hughes (2002)
Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.Journal of molecular biology, 318 4
G. Fraser, T. Hirano, H. Ferris, Lara Devgan, M. Kihara, R. Macnab (2003)
Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhBMolecular Microbiology, 48
B. González-Pedrajo, G. Fraser, T. Minamino, R. Macnab (2002)
Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathwayMolecular Microbiology, 45
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 (FlhAC). FlhAC and a 38 kDa fragment of FlhAC (FlhAC38K) were purified and crystallized. The crystals were obtained by the sitting‐drop vapour‐diffusion technique with PEG 8000 as a precipitant. FlhAC crystals grew in the tetragonal space group I41/I43, with unit‐cell parameters a = b = 216.6, c = 65.0 Å. FlhAC38K 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 FlhAC and the SeMet derivative of FlhAC were collected to 2.9 and 3.2 Å, respectively.
Acta Crystallographica Section F – Wiley
Published: Jun 1, 2005
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