title: Structural and functional analyses of mutant Fur proteins with impaired regulatory function.
abstract: Vibrio anguillarum Fur mutants, 775met9 and 775met11, were characterized. V. anguillarum 775met9 had a change of D to G at position 104 located in the carboxy terminus resulting in impaired Fur activity. Computer analysis predicts perturbation of an alpha-helix in the carboxy terminus which may interfere with Fur protein conformation. Strain 775met11 had a change in the start codon resulting in no protein synthesis. The mutants are unstable, and reversion to the wild type occurs frequently.
authors.affiliation: Department of Molecular Microbiology and Immunology, School of Medicine, Oregon Health Sciences University, Portland 97201-3098.
authors.forename: A M
authors.initials: AM
authors.lastname: Wertheimer
authors.forename: M E
authors.initials: ME
authors.lastname: Tolmasky
authors.forename: L A
authors.initials: LA
authors.lastname: Actis
authors.forename: J H
authors.initials: JH
authors.lastname: Crosa
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D003001:Cloning, Molecular; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D007501:Iron / Q000378:metabolism; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D014733:Vibrio / Q000235:genetics*
chemical_list: D001426:Bacterial Proteins; D012097:Repressor Proteins; C068477:ferric uptake regulating proteins, bacterial; D007501:Iron