PDBsum entry 2mc7

Membrane protein

PDB id: 2mc7

Contents

Protein chain

30 a.a.

PDB id:

2mc7

Name:

Membrane protein

Title:

Structure of salmonella mgtr

Structure:

Regulatory peptide. Chain: a. Engineered: yes

Source:

Synthetic: yes. Salmonella typhimurium. Organism_taxid: 90371

NMR struc:

1 models

Authors:

F.Jean-Francois,J.Dai,L.Yu,A.Myrick,E.Rubin,P.Fajer,L.Song,H.Zhou, T.Cross

Key ref:

F.L.Jean-Francois et al. (2014). Binding of MgtR, a Salmonella transmembrane regulatory peptide, to MgtC, a Mycobacterium tuberculosis virulence factor: a structural study. J Mol Biol, 426, 436-446. PubMed id: 24140750 DOI: 10.1016/j.jmb.2013.10.014

Date:

15-Aug-13 Release date: 30-Oct-13

Protein chain

B0LJC7  (B0LJC7_SALTM) -  Protein MgtR from Salmonella typhimurium

Seq: 30 a.a.

Struc: 30 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2013.10.014

J Mol Biol 426:436-446 (2014)

PubMed id: 24140750

Binding of MgtR, a Salmonella transmembrane regulatory peptide, to MgtC, a Mycobacterium tuberculosis virulence factor: a structural study.

F.L.Jean-Francois, J.Dai, L.Yu, A.Myrick, E.Rubin, P.G.Fajer, L.Song, H.X.Zhou, T.A.Cross.

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.