2NC8

NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain

2NC8 の概要

• エントリーDOI: 10.2210/pdb2nc8/pdb
• NMR情報: BMRB: 26010
• 分子名称: Lipoprotein LppM (1 entity in total)
• 機能のキーワード: transport protein, protein binding
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19417.47

構造登録者

Barthe, P.,Cohen-Gonsaud, M. (登録日: 2016-03-22, 公開日: 2016-09-14, 最終更新日: 2024-05-15)

主引用文献

Barthe, P.,Veyron-Churlet, R.,de Visch, A.,Gilleron, M.,Saliou, J.M.,Tomavo, S.,Nigou, J.,Brodin, P.,Cohen-Gonsaud, M.
Mycobacterium tuberculosis LppM Displays an Original Structure and Domain Composition Linked to a Dual Localization.
Structure, 24:1788-1794, 2016

PubMed Abstract: Mycobacterium tuberculosis (Mtb) encodes several bacterial effectors impacting the colonization of phagocytes. LppM (Rv2171) is both implicated in phagocytosis and able to efficiently block phagosomal acidification in the macrophage, two key processes contributing to Mtb persistence. We show that LppM is anchored to the mycobacterial cell wall by a C-terminal membrane domain. However, the protein also exists as a truncated protein secreted into the culture medium. The LppM solution structure we solve here displays no similarity with other Mtb lipoproteins also involved in phagosomal maturation (i.e., LprG). In addition, we demonstrate that the protein may be able to bind rare molecular species of phosphatidylinositol mannosides, bacterial compounds known to affect the host immune response. Thus, our data demonstrate a dual localization of LppM and provide a unique perspective on the regulation of protein secretion and localization in Mtb.

PubMed: 27568926
DOI: 10.1016/j.str.2016.07.009

実験手法

SOLUTION NMR