Binding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural Study
| Autor: | Likai Song, Huan-Xiang Zhou, Frantz Jean-Francois, Alissa Myrick, Eric J. Rubin, Lu Yu, Piotr G. Fajer, Jian Dai, Timothy A. Cross |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Salmonella typhimurium Magnetic Resonance Spectroscopy Protein Conformation Lipid Bilayers Plasma protein binding Article Virulence factor Mycobacterium tuberculosis Protein structure Bacterial Proteins Structural Biology Protein Interaction Mapping Molecular Biology biology Chemistry Electron Spin Resonance Spectroscopy biology.organism_classification Transmembrane protein Transmembrane domain Membrane protein Biochemistry Salmonella enterica Protein Multimerization Protein Binding |
| Zdroj: | Journal of Molecular Biology. 426:436-446 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2013.10.014 |
| Popis: | 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 homologuous to its S. Typhimurium 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. Typhimurium 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect