6kz4

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Current revision (05:48, 3 July 2025) (edit) (undo)
 
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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=6kz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kz4 OCA], [https://pdbe.org/6kz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kz4 RCSB], [https://www.ebi.ac.uk/pdbsum/6kz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kz4 ProSAT]</span></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=6kz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kz4 OCA], [https://pdbe.org/6kz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kz4 RCSB], [https://www.ebi.ac.uk/pdbsum/6kz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kz4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/YEBT_ECOLI YEBT_ECOLI] Component of a transport pathway that contributes to membrane integrity (PubMed:27795327). May directly span the intermembrane space, facilitating the transport of substrates across the periplasm (Probable).<ref>PMID:27795327</ref> <ref>PMID:28388411</ref>
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== Publication Abstract from PubMed ==
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The outer membrane (OM) of Gram-negative bacteria is asymmetric, with lipopolysaccharides (LPSs) on the outer surface and phospholipids (PLs) on the inner surface. This unique organization of OM makes Gram-negative bacteria resistant to many toxic chemicals. How this asymmetric distribution of lipids is maintained has been studied for decades with previous reports of an Mla (Maintenance of OM Lipid Asymmetry) system to be involved. Furthermore, the OM of Gram-negative bacteria is about 20 nm away from inner membrane (IM) where the lipids are synthesized. Therefore, how nascent lipids travel across the periplasmic space and arrive at the inner surface of OM is another interesting question. YebT is a homologue of MlaD in the Mla pathway, but its role in lipid distribution of the OM and IM is largely unknown. Here we report the first high-resolution (~3.0 A) cryo-EM structure of full-length E. coli YebT in a substrate-bound state. Our structure with details of lipid interaction indicates that YebT is a lipid transporter spanning between IM and OM. We also demonstrate the symmetry mismatch in YebT and the existence of many other conformations of YebT revealing the intrinsic dynamics of this lipid channel. And a brief discussion on possible mechanisms of lipid transport is also included.
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Cryo-EM Structure of a Bacterial Lipid Transporter YebT.,Liu C, Ma J, Wang J, Wang H, Zhang L J Mol Biol. 2020 Feb 14;432(4):1008-1019. doi: 10.1016/j.jmb.2019.12.008. Epub, 2019 Dec 21. PMID:31870848<ref>PMID:31870848</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6kz4" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Current revision

YebT domain 5-7

6kz4, resolution 3.00Å

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