title: Method for the Successful Crystallization of the Ferric Uptake Regulator from Campylobacter jejuni.
abstract: The Ferric Uptake Regulator (FUR) is a transcription factor (TF) regulating the expression of several genes to control iron levels in prokaryotes. Members of this family of TFs share a common structural scaffold that typically comprises two regions that include a DNA binding and dimerization domains. While this structural organization is conserved, FUR proteins employ different mechanisms to bind divergent DNA binding elements and regulate gene expression in the absence or presence of regulatory metals. These findings, combined with the observations that FUR proteins display different geometries in regard to the relative orientation of the DNA binding and dimerization domains, have highlighted an expanding repertoire of molecular mechanisms controlling the activity of this family of TFs. In this chapter, we present an overview of the methods to purify, crystallize, and solve the structure of Campylobacter jejuni FUR.
authors.affiliation: Ottawa Institute of Systems Biology, University of Ottawa, Roger Guindon Hall, 451 Smyth Road, Ottawa, ON, Canada, K1H 8M5.|Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Roger Guindon Hall, 451 Smyth Road, Ottawa, ON, Canada, K1H 8M5.
authors.forename: Sabina
authors.initials: S
authors.lastname: Sarvan
authors.affiliation: Ottawa Institute of Systems Biology, University of Ottawa, Roger Guindon Hall, 451 Smyth Road, Ottawa, ON, Canada, K1H 8M5.|Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Roger Guindon Hall, 451 Smyth Road, Ottawa, ON, Canada, K1H 8M5.
authors.forename: Jean-François
authors.initials: JF
authors.lastname: Couture
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D016123:Campylobacter jejuni / Q000235:genetics* / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods; D003001:Cloning, Molecular; D003451:Cryoprotective Agents / Q000737:chemistry; D003460:Crystallization / Q000379:methods; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D019855:Ethylene Glycol / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial; D007501:Iron / Q000737:chemistry* / Q000378:metabolism; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D003451:Cryoprotective Agents; D011994:Recombinant Proteins; D012097:Repressor Proteins; C068477:ferric uptake regulating proteins, bacterial; D004247:DNA; D007501:Iron; D019855:Ethylene Glycol
keywords: Apo-metalloregulator; Bacterial metalloregulator; Fur; Strep-tag affinity chromatography; Transcription factor