2MC7
Structure of Salmonella MgtR
Summary for 2MC7
| Entry DOI | 10.2210/pdb2mc7/pdb |
| NMR Information | BMRB: 19430 |
| Descriptor | Regulatory peptide (1 entity in total) |
| Functional Keywords | transmembrane helical complex, membrane protein |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 1 |
| Total formula weight | 3459.34 |
| Authors | Jean-Francois, F.,Dai, J.,Yu, L.,Myrick, A.,Rubin, E.,Fajer, P.,Song, L.,Zhou, H.,Cross, T. (deposition date: 2013-08-15, release date: 2013-10-30, Last modification date: 2024-05-01) |
| Primary citation | Jean-Francois, F.L.,Dai, J.,Yu, L.,Myrick, A.,Rubin, E.,Fajer, P.G.,Song, L.,Zhou, H.X.,Cross, T.A. Binding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural Study. J.Mol.Biol., 426:436-446, 2014 Cited by PubMed 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. PubMed: 24140750DOI: 10.1016/j.jmb.2013.10.014 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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