Binding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural Study
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Publication Details
Output type: Journal article
Author list: Jean-Francois FL, Dai J, Yu L, Myrick A, Rubin E, Fajer PG, Song L, Zhou HX, Cross TA
Publisher: Elsevier
Publication year: 2014
Journal: Journal of Molecular Biology (0022-2836)
Volume number: 426
Issue number: 2
Start page: 436
End page: 446
Number of pages: 11
ISSN: 0022-2836
Languages: English-Great Britain (EN-GB)
Unpaywall Data
Open access status: green
Full text URL: https://europepmc.org/articles/pmc3947350?pdf=render
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. (C) 2013 Elsevier Ltd. All rights reserved.
Keywords
distance restraints, electron spin resonance, orientational restraints, restrained molecular dynamics, solid-state nuclear magnetic resonance
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