Understanding the Potential Interaction of Transmembrane Helices from MgtC and MgtR
| Autor: | Timothy A. Cross, Frantz Jean-Francois |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Protein dynamics Biophysics Peptide Biology medicine.disease_cause biology.organism_classification Amino acid 03 medical and health sciences Transmembrane domain 0302 clinical medicine Membrane Membrane protein chemistry Biochemistry medicine Escherichia coli 030217 neurology & neurosurgery Bacteria 030304 developmental biology |
| Zdroj: | Biophysical Journal. 100:384a-385a |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/j.bpj.2010.12.2287 |
| Popis: | Beyond the challenge consisting of solving a membrane protein structure, Solid state NMR is the most powerful technique to decipher protein dynamics within the membrane hydrophobic core. Recent results have converged to highlight the role of hydrophobic peptides that form a novel class of active molecules in Escherichia coli and Salmonella enteric serovar Typhimurium. These peptides are apparently able to interact with membrane proteins leading to their inactivation through an unfolding process. Understanding the molecular mechanism of these peptide-protein interactions would offer great opportunities in pharmacology and drug design.MgtR, a highly hydrophobic 30 amino acids peptide, which is expressed in Salmonella typhimurium, is one of these active molecules. It has been shown that within the macrophage, the over expression of MgtR leads to a decrease of Salmonella replication rate. This process was shown to involve an interaction between MgtR and a membrane protein of Salmollena (MgtC) which is required for the bacteria survival at low magnesium concentration. Throughout the literature, MgtC has proven to be one of the key factors in Mycobaterium tuberculosis latent state. Relying on the sequence homology between Salmonella typhimurium MgtC and Mycobacterium tuberculosis MgtC, the interaction between MgtR from Salmonella typhimurium and the transmembrane domain #4 of Mycobacterium tuberculosis MgtC will be studied.Structural studies using solid state NMR methods such as CP-MAS and PI SEMA on oriented samples have been performed. Several 15N labeled peptides were produced by chemical synthesis and biological expression prior reconstitution into model membranes. These NMR studies allowed us to determine theses peptides topology and their backbone structure within membranes. Interaction studies between these two peptides are currently in progress and will allow us to define the complex structure as well as the amino acids involved in the interaction. |
| Databáze: | OpenAIRE |
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