Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 426, Issue 2, Pages 436-446Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2013.10.014
Keywords
solid-state nuclear magnetic resonance; electron spin resonance; restrained molecular dynamics; orientational restraints; distance restraints
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Funding
- National Institutes of Health [AI074805, GM088187]
- State of Florida [DMR-1157490]
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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.
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