6vci
From Proteopedia
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==Lipophilic envelope-spanning tunnel protein (LetB), domains MCE2-MCE3== | ==Lipophilic envelope-spanning tunnel protein (LetB), domains MCE2-MCE3== | ||
| - | <StructureSection load='6vci' size='340' side='right'caption='[[6vci]]' scene=''> | + | <StructureSection load='6vci' size='340' side='right'caption='[[6vci]], [[Resolution|resolution]] 2.15Å' 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=6VCI OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6vci]] is a 2 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=6VCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VCI FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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=6vci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vci OCA], [https://pdbe.org/6vci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vci RCSB], [https://www.ebi.ac.uk/pdbsum/6vci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vci ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6vci" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bhabha G]] | [[Category: Bhabha G]] | ||
Current revision
Lipophilic envelope-spanning tunnel protein (LetB), domains MCE2-MCE3
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