7k7m
From Proteopedia
(Difference between revisions)
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==Crystal Structure of a membrane protein== | ==Crystal Structure of a membrane protein== | ||
| - | <StructureSection load='7k7m' size='340' side='right'caption='[[7k7m]]' scene=''> | + | <StructureSection load='7k7m' size='340' side='right'caption='[[7k7m]], [[Resolution|resolution]] 3.33Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K7M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7k7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K7M FirstGlance]. <br> |
| - | </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=7k7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k7m OCA], [https://pdbe.org/7k7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k7m RCSB], [https://www.ebi.ac.uk/pdbsum/7k7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k7m ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.33Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900093:6-decanoyl-trehalose'>PRD_900093</scene>, <scene name='pdbligand=U2D:6-O-decanoyl-alpha-D-glucopyranose'>U2D</scene></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=7k7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k7m OCA], [https://pdbe.org/7k7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k7m RCSB], [https://www.ebi.ac.uk/pdbsum/7k7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k7m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MMPL3_MYCS2 MMPL3_MYCS2] Transports trehalose monomycolate (TMM) to the cell wall (PubMed:31239378, PubMed:22520756, PubMed:28698380). Flips TMM across the inner membrane. Membrane potential is not required for this function (PubMed:28698380). Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL) (PubMed:31113875). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness (PubMed:28703701).<ref>PMID:22520756</ref> <ref>PMID:28698380</ref> <ref>PMID:28703701</ref> <ref>PMID:31113875</ref> <ref>PMID:31239378</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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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| + | 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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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7k7m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Mycolicibacterium smegmatis MC2 155]] | ||
[[Category: Su C-C]] | [[Category: Su C-C]] | ||
Current revision
Crystal Structure of a membrane protein
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