2nc8

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

spinqualitylabelsall models 2nc8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nc8 is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LPPM_MYCTU A putative lipoprotein that seems to be specialized for the initial steps of macrophage infection (PubMed:27220037). A non-acylated fragment (residues 26-185) binds phosphatidyl-myo-inositol mannosides (PIMs) (PubMed:27568926). Limits, in a TLR2-dependent fashion, bacterial uptake by host (mouse); this effect may be mediated by nonacylated fragment 26-185 (PubMed:27220037). Plays a TLR2-dependent role in host phagosome maturation arrest (PubMed:20844580, PubMed:27220037). Plays a TLR2-independent role in chemokine production during the first 24 hours of mouse infection (PubMed:27220037). Publication Abstract from PubMed 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. Mycobacterium tuberculosis LppM Displays an Original Structure and Domain Composition Linked to a Dual Localization.,Barthe P, Veyron-Churlet R, de Visch A, Gilleron M, Saliou JM, Tomavo S, Nigou J, Brodin P, Cohen-Gonsaud M Structure. 2016 Aug 23. pii: S0969-2126(16)30220-9. doi:, 10.1016/j.str.2016.07.009. PMID:27568926 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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