title: Preparation and preliminary X-ray diffraction analysis of crystals of bacterial flagellar sigma factor sigma 28 in complex with the sigma 28-binding region of its antisigma factor, FlgM.
abstract: The sigma 28 kDa (sigma28) factor is a transcription factor specific for the expression of bacterial flagellar and chemotaxis genes. Its antisigma factor, FlgM, binds sigma28 factor and inhibits its activity as a transcription factor. In this study, crystals of the complex between Escherichia coli sigma28 and the C-terminal sigma28-binding region of FlgM were obtained. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 106.7 (2), c = 51.74 (3) A, containing one complex in the crystallographic asymmetric unit. An X-ray intensity data set was collected to a resolution of 2.7 A.
authors.affiliation: Structural Biology Laboratory, Nara Institute of Science and Technology, Keihanna Science City, Nara 630-0192, Japan.
authors.forename: Kengo
authors.initials: K
authors.lastname: Okada
authors.forename: Hisako
authors.initials: H
authors.lastname: Ichihara
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Takahashi
authors.forename: Nobuyuki
authors.initials: N
authors.lastname: Fujita
authors.forename: Akira
authors.initials: A
authors.lastname: Ishihama
authors.forename: Toshio
authors.initials: T
authors.lastname: Hakoshima
mesh_terms: D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D001667:Binding, Competitive; D002478:Cells, Cultured; D002633:Chemotaxis; D003460:Crystallization; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D005407:Flagella / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D012808:Sigma Factor / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; C064971:FliA protein, Bacteria; D012808:Sigma Factor; C071266:FlgM protein, Bacteria