6vci: Difference between revisions

Latest revision as of 08:08, 11 October 2023

Lipophilic envelope-spanning tunnel protein (LetB), domains MCE2-MCE3

Structural highlights

6vci is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.15Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nakayama T, Zhang-Akiyama QM. pqiABC and yebST, Putative mce Operons of Escherichia coli, Encode Transport Pathways and Contribute to Membrane Integrity. J Bacteriol. 2016 Dec 13;199(1). pii: JB.00606-16. doi: 10.1128/JB.00606-16., Print 2017 Jan 1. PMID:27795327 doi:https://dx.doi.org/10.1128/JB.00606-16
↑ Ekiert DC, Bhabha G, Isom GL, Greenan G, Ovchinnikov S, Henderson IR, Cox JS, Vale RD. Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell. 2017 Apr 6;169(2):273-285.e17. doi: 10.1016/j.cell.2017.03.019. PMID:28388411 doi:https://dx.doi.org/10.1016/j.cell.2017.03.019
↑ Isom GL, Coudray N, MacRae MR, McManus CT, Ekiert DC, Bhabha G. LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope. Cell. 2020 Apr 30;181(3):653-664.e19. doi: 10.1016/j.cell.2020.03.030. PMID:32359438 doi:https://dx.doi.org/10.1016/j.cell.2020.03.030

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OCA

[1] Nakayama T, Zhang-Akiyama QM. pqiABC and yebST, Putative mce Operons of Escherichia coli, Encode Transport Pathways and Contribute to Membrane Integrity. J Bacteriol. 2016 Dec 13;199(1). pii: JB.00606-16. doi: 10.1128/JB.00606-16., Print 2017 Jan 1. PMID:27795327 doi:https://dx.doi.org/10.1128/JB.00606-16

[2] Ekiert DC, Bhabha G, Isom GL, Greenan G, Ovchinnikov S, Henderson IR, Cox JS, Vale RD. Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell. 2017 Apr 6;169(2):273-285.e17. doi: 10.1016/j.cell.2017.03.019. PMID:28388411 doi:https://dx.doi.org/10.1016/j.cell.2017.03.019

[3] Isom GL, Coudray N, MacRae MR, McManus CT, Ekiert DC, Bhabha G. LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope. Cell. 2020 Apr 30;181(3):653-664.e19. doi: 10.1016/j.cell.2020.03.030. PMID:32359438 doi:https://dx.doi.org/10.1016/j.cell.2020.03.030

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6vci is ON HOLD
+==Lipophilic envelope-spanning tunnel protein (LetB), domains MCE2-MCE3==
+<StructureSection load='6vci' size='340' side='right'caption='[[6vci]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</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>
+== 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.
-Authors: Isom, G.L., Coudray, N., MacRae, M.R., McManus, C.T., Ekiert, D.C., Bhabha, G.
+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>
-Description: LetB MCE2-MCE3 crystal structure
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Ekiert, D.C]]
+<div class="pdbe-citations 6vci" style="background-color:#fffaf0;"></div>
-[[Category: Isom, G.L]]
+== References ==
-[[Category: Bhabha, G]]
+<references/>
-[[Category: Coudray, N]]
+__TOC__
-[[Category: Macrae, M.R]]
+</StructureSection>
-[[Category: Mcmanus, C.T]]
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Bhabha G]]
+[[Category: Coudray N]]
+[[Category: Ekiert DC]]
+[[Category: Isom GL]]
+[[Category: MacRae MR]]
+[[Category: McManus CT]]

6vci: Difference between revisions

Latest revision as of 08:08, 11 October 2023

Lipophilic envelope-spanning tunnel protein (LetB), domains MCE2-MCE3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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