2NC8
NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain
Summary for 2NC8
| Entry DOI | 10.2210/pdb2nc8/pdb |
| NMR Information | BMRB: 26010 |
| Descriptor | Lipoprotein LppM (1 entity in total) |
| Functional Keywords | transport protein, protein binding |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 19417.47 |
| Authors | Barthe, P.,Cohen-Gonsaud, M. (deposition date: 2016-03-22, release date: 2016-09-14, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 27568926DOI: 10.1016/j.str.2016.07.009 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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