2nc8

From Proteopedia

(Difference between revisions)

Current revision

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

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).^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barthe P, Veyron-Churlet R, de Visch A, Gilleron M, Saliou JM, 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. 2016 Aug 23. pii: S0969-2126(16)30220-9. doi:, 10.1016/j.str.2016.07.009. PMID:27568926 doi:http://dx.doi.org/10.1016/j.str.2016.07.009
↑ Brodin P, Poquet Y, Levillain F, Peguillet I, Larrouy-Maumus G, Gilleron M, Ewann F, Christophe T, Fenistein D, Jang J, Jang MS, Park SJ, Rauzier J, Carralot JP, Shrimpton R, Genovesio A, Gonzalo-Asensio JA, Puzo G, Martin C, Brosch R, Stewart GR, Gicquel B, Neyrolles O. High content phenotypic cell-based visual screen identifies Mycobacterium tuberculosis acyltrehalose-containing glycolipids involved in phagosome remodeling. PLoS Pathog. 2010 Sep 9;6(9):e1001100. PMID:20844580 doi:10.1371/journal.ppat.1001100
↑ Deboosère N, Iantomasi R, Queval CJ, Song OR, Deloison G, Jouny S, Debrie AS, Chamaillard M, Nigou J, Cohen-Gonsaud M, Locht C, Brodin P, Veyron-Churlet R. LppM impact on the colonization of macrophages by Mycobacterium tuberculosis. Cell Microbiol. 2017 Jan;19(1):e12619. PMID:27220037 doi:10.1111/cmi.12619
↑ Barthe P, Veyron-Churlet R, de Visch A, Gilleron M, Saliou JM, 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. 2016 Aug 23. pii: S0969-2126(16)30220-9. doi:, 10.1016/j.str.2016.07.009. PMID:27568926 doi:http://dx.doi.org/10.1016/j.str.2016.07.009

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nc8"

Categories: Large Structures | Mycobacterium tuberculosis | Barthe P | Cohen-Gonsaud M

@@ Line 1: / Line 1: @@
-{{Large structure}}
 ==NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain==
-<StructureSection load='2nc8' size='340' side='right' caption='[[2nc8]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<StructureSection load='2nc8' size='340' side='right'caption='[[2nc8]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2nc8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NC8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NC8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2nc8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NC8 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc8 OCA], [http://pdbe.org/2nc8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nc8 RCSB], [http://www.ebi.ac.uk/pdbsum/2nc8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nc8 ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc8 OCA], [https://pdbe.org/2nc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nc8 RCSB], [https://www.ebi.ac.uk/pdbsum/2nc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nc8 ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
+== Function ==
+[https://www.uniprot.org/uniprot/LPPM_MYCTU 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).<ref>PMID:27568926</ref> <ref>PMID:20844580</ref> <ref>PMID:27220037</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Barthe, P]]
+[[Category: Large Structures]]
-[[Category: Cohen-Gonsaud, M]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Protein binding]]
+[[Category: Barthe P]]
-[[Category: Transport protein]]
+[[Category: Cohen-Gonsaud M]]

2nc8

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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