2MC7

Structure of Salmonella MgtR

2MC7 の概要

• エントリーDOI: 10.2210/pdb2mc7/pdb
• NMR情報: BMRB: 19430
• 分子名称: Regulatory peptide (1 entity in total)
• 機能のキーワード: transmembrane helical complex, membrane protein
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3459.34

構造登録者

Jean-Francois, F.,Dai, J.,Yu, L.,Myrick, A.,Rubin, E.,Fajer, P.,Song, L.,Zhou, H.,Cross, T. (登録日: 2013-08-15, 公開日: 2013-10-30, 最終更新日: 2024-05-01)

主引用文献

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

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: 24140750
DOI: 10.1016/j.jmb.2013.10.014

実験手法

SOLID-STATE NMR