Functional analysis of the conserved hydrophobic gate region of the magnesium transporter CorA

Soňa Svidová; Gerhard Sponder; Rudolf J Schweyen; Kristina Djinović-Carugo

doi:10.1016/j.bbamem.2010.10.017

Functional analysis of the conserved hydrophobic gate region of the magnesium transporter CorA

Biochim Biophys Acta. 2011 Jun;1808(6):1587-91. doi: 10.1016/j.bbamem.2010.10.017. Epub 2010 Nov 11.

Authors

Soňa Svidová¹, Gerhard Sponder, Rudolf J Schweyen, Kristina Djinović-Carugo

Affiliation

¹ Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, University of Vienna, Dr. Bohrgasse 9/4, A-1030 Vienna, Austria.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Substitution
Aspartic Acid / genetics
Bacterial Proteins / chemistry
Bacterial Proteins / genetics
Bacterial Proteins / physiology*
Blotting, Western
Cation Transport Proteins / chemistry
Cation Transport Proteins / genetics
Cation Transport Proteins / physiology*
Glycine / genetics
Hydrophobic and Hydrophilic Interactions
Ion Transport
Leucine / genetics
Magnesium / metabolism*
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Conformation
Thermotoga maritima / metabolism*

Substances

Bacterial Proteins
Cation Transport Proteins
Aspartic Acid
Leucine
Magnesium
Glycine