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6v0h

From Proteopedia

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Current revision (14:35, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6v0h' size='340' side='right'caption='[[6v0h]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='6v0h' size='340' side='right'caption='[[6v0h]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6v0h]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V0H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V0H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6v0h]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V0H FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yebT, b1834, JW1823 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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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]] 3.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v0h OCA], [http://pdbe.org/6v0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v0h RCSB], [http://www.ebi.ac.uk/pdbsum/6v0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v0h ProSAT]</span></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=6v0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v0h OCA], [https://pdbe.org/6v0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v0h RCSB], [https://www.ebi.ac.uk/pdbsum/6v0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v0h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Gram-negative bacteria are surrounded by an outer membrane composed of phospholipids and lipopolysaccharide, which acts as a barrier and contributes to antibiotic resistance. The systems that mediate phospholipid trafficking across the periplasm, such as MCE (Mammalian Cell Entry) transporters, have not been well characterized. Our ~3.5 A cryo-EM structure of the E. coli MCE protein LetB reveals an ~0.6 megadalton complex that consists of seven stacked rings, with a central hydrophobic tunnel sufficiently long to span the periplasm. Lipids bind inside the tunnel, suggesting that it functions as a pathway for lipid transport. Cryo-EM structures in the open and closed states reveal a dynamic tunnel lining, with implications for gating or substrate translocation. Our results support a model in which LetB establishes a physical link between the two membranes and creates a hydrophobic pathway for the translocation of lipids across the periplasm.
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LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope.,Isom GL, Coudray N, MacRae MR, McManus CT, Ekiert DC, Bhabha G Cell. 2020 Apr 30;181(3):653-664.e19. doi: 10.1016/j.cell.2020.03.030. PMID:32359438<ref>PMID:32359438</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 6v0h" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhabha, G]]
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[[Category: Bhabha G]]
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[[Category: Coudray, N]]
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[[Category: Coudray N]]
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[[Category: Ekiert, D C]]
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[[Category: Ekiert DC]]
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[[Category: Isom, G L]]
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[[Category: Isom GL]]
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[[Category: MacRae, M R]]
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[[Category: MacRae MR]]
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[[Category: McManus, C T]]
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[[Category: McManus CT]]
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[[Category: Bacterial cell envelope]]
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[[Category: Conformational dynamic]]
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[[Category: Letb]]
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[[Category: Lipid transport]]
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[[Category: Mce]]
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[[Category: Yebt]]
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Current revision

Lipophilic Envelope-spanning Tunnel B (LetB), Model 6

PDB ID 6v0h

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