title: Functional analysis of the conserved hydrophobic gate region of the magnesium transporter CorA.
abstract: The Leu294 residue in the cytoplasmic neck of Thermotoga maritima CorA is considered to be the main gate for Mg2+ transport. We created three site-directed mutants at this position: in the Leu294Asp and Leu294Gly mutants we observed a defect in closing of the pore, while in the Leu294Arg mutant not only gating, but also the regulation of Mg2+ uptake was affected. Our results confirmed the importance of the Leu294 for gating of Mg2+ transport and in addition revealed the influence of the charge and structural features of the amino acid residues on the gating mechanism.
authors.affiliation: Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, University of Vienna, Dr. Bohrgasse 9/4, A-1030 Vienna, Austria.
authors.forename: Soňa
authors.initials: S
authors.lastname: Svidová
authors.forename: Gerhard
authors.initials: G
authors.lastname: Sponder
authors.forename: Rudolf J
authors.initials: RJ
authors.lastname: Schweyen
authors.forename: Kristina
authors.initials: K
authors.lastname: Djinović-Carugo
mesh_terms: D019943:Amino Acid Substitution; D001224:Aspartic Acid / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D015153:Blotting, Western; D027682:Cation Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D005998:Glycine / Q000235:genetics; D057927:Hydrophobic and Hydrophilic Interactions; D017136:Ion Transport; D007930:Leucine / Q000235:genetics; D008274:Magnesium / Q000378:metabolism*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011487:Protein Conformation; D020124:Thermotoga maritima / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D001224:Aspartic Acid; D007930:Leucine; D008274:Magnesium; D005998:Glycine