Binding of MgtR,a Salmonella Transmembrane Regulatory Peptide,to MgtC,a Mycobacterium tuberculosis Virulence Factor: A Structural Study |
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| Authors: | Frantz L. Jean-Francois Jian Dai Lu Yu Alissa Myrick Eric Rubin Piotr G. Fajer Likai Song Huan-Xiang Zhou Timothy A. Cross |
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| Affiliation: | 1 National High Magnetic Field Laboratory, Tallahassee, FL 32306, USA;2 Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, USA;3 Department of Physics, Florida State University, Tallahassee, FL 32306, USA;4 Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA;5 University of Science and Technology of China, Hefei 230031, China;6 Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02138, USA |
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| Abstract: | MgtR, a highly hydrophobic peptide expressed in Salmonella enterica serovar Typhimurium, inhibits growth in macrophages through binding to the membrane protein MgtC that has been identified as essential for replication in macrophages. While the Mycobacterium tuberculosis MgtC is highly homologous to its S. Typhi analogue, there does not appear to be an Mtb homologue for MgtR, raising significant pharmacological interest in this system. Here, solid-state NMR and EPR spectroscopy in lipid bilayer preparations were used to demonstrate the formation of a heterodimer between S. Typhi MgtR and the transmembrane helix 4 of Mtb MgtC. Based on the experimental restraints, a structural model of this heterodimer was developed using computational techniques. The result is that MgtR appears to be ideally situated in the membrane to influence the functionality of MgtC. |
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| Keywords: | PISEMA, polarization inversion spin exchange at the magic angle MD, molecular dynamics |
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