2nc8: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

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

== 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>

</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>

</table>

== 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.

~~The entry 2nc8 is ON HOLD until Paper Publication~~

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<ref>PMID:27568926</ref>

~~Authors: Barthe~~, P.~~, Cohen-Gonsaud, M~~.

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

</div>

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

[[Category: ~~Unreleased Structures~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Barthe, P]]

[[Category: Cohen-Gonsaud, M]]

[[Category: ~~Barthe, P~~]]

[[Category: Protein binding]]

[[Category: Transport protein]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{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=''>
+== 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>
+</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>
+</table>
+{{Large structure}}
+<div style="background-color:#fffaf0;">
+== 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.
-The entry 2nc8 is ON HOLD  until Paper Publication
+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<ref>PMID:27568926</ref>
-Authors: Barthe, P., Cohen-Gonsaud, M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain
+<div class="pdbe-citations 2nc8" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Barthe, P]]
 [[Category: Cohen-Gonsaud, M]]
-[[Category: Barthe, P]]
+[[Category: Protein binding]]
+[[Category: Transport protein]]