7k8c

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'''Unreleased structure'''
 
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The entry 7k8c is ON HOLD
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==CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs==
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<StructureSection load='7k8c' size='340' side='right'caption='[[7k8c]], [[Resolution|resolution]] 4.27&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K8C FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.27&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7k8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k8c OCA], [https://pdbe.org/7k8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k8c RCSB], [https://www.ebi.ac.uk/pdbsum/7k8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k8c ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mycobacterial membrane protein large 3 (MmpL3) transporter is essential and required for shuttling the lipid trehalose monomycolate (TMM), a precursor of mycolic acid (MA)-containing trehalose dimycolate (TDM) and mycolyl arabinogalactan peptidoglycan (mAGP), in Mycobacterium species, including Mycobacterium tuberculosis and Mycobacterium smegmatis. However, the mechanism that MmpL3 uses to facilitate the transport of fatty acids and lipidic elements to the mycobacterial cell wall remains elusive. Here, we report 7 structures of the M. smegmatis MmpL3 transporter in its unbound state and in complex with trehalose 6-decanoate (T6D) or TMM using single-particle cryo-electron microscopy (cryo-EM) and X-ray crystallography. Combined with calculated results from molecular dynamics (MD) and target MD simulations, we reveal a lipid transport mechanism that involves a coupled movement of the periplasmic domain and transmembrane helices of the MmpL3 transporter that facilitates the shuttling of lipids to the mycobacterial cell wall.
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Authors: Su, C.-C.
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Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport.,Su CC, Klenotic PA, Cui M, Lyu M, Morgan CE, Yu EW PLoS Biol. 2021 Aug 12;19(8):e3001370. doi: 10.1371/journal.pbio.3001370., eCollection 2021 Aug. PMID:34383749<ref>PMID:34383749</ref>
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Description: CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Su, C.-C]]
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<div class="pdbe-citations 7k8c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Su C-C]]

Current revision

CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs

PDB ID 7k8c

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