9fz5

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of LptDE-YedD complex from Escherichia Coli

Structural highlights

9fz5 is a 3 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:	Electron Microscopy, Resolution 3.57Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LPTD_ECOLI Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance.[HAMAP-Rule:MF_01411]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

The outer membrane is an efficient permeability barrier that protects gram-negative bacteria against external assaults, including many antibiotics. The unique permeability features of the outer membrane are due to the presence of lipopolysaccharide (LPS) molecules in its outer leaflet. LPS transport relies on the essential lipopolysaccharide transport (Lpt) pathway, which forms a bridge from the inner to the outer membrane. The LptDE translocon inserts LPS into the outer leaflet. Here, we identify the lipocalin YedD as a component of the translocon. Cryoelectron microscopy of the YedD-LptDE complex reveals that YedD binds LptD at a critical interface between its beta-barrel and periplasmic beta-taco domain. The YedD-LptDE complex is functionally relevant: under conditions where the connectivity of the beta-taco and Lpt bridge is compromised, the absence of YedD decreases cell viability and causes LPS accumulation in the inner membrane. Our findings establish YedD as an Lpt component required for optimal LPS transport.

Optimal functioning of the Lpt bridge depends on a ternary complex between the lipocalin YedD and the LptDE translocon.,Gennaris A, Nguyen VS, Thouvenel L, Csoma N, Vertommen D, Iorga BI, Remaut H, Collet JF Cell Rep. 2025 Mar 23;44(4):115446. doi: 10.1016/j.celrep.2025.115446. PMID:40127101^[9]

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

References

↑ Braun M, Silhavy TJ. Imp/OstA is required for cell envelope biogenesis in Escherichia coli. Mol Microbiol. 2002 Sep;45(5):1289-302. PMID:12207697
↑ Abe S, Okutsu T, Nakajima H, Kakuda N, Ohtsu I, Aono R. n-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDa minor protein associated with the outer membrane. Microbiology. 2003 May;149(Pt 5):1265-73. PMID:12724388
↑ Wu T, McCandlish AC, Gronenberg LS, Chng SS, Silhavy TJ, Kahne D. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11754-9. Epub 2006 Jul 21. PMID:16861298 doi:http://dx.doi.org/0604744103
↑ Sperandeo P, Lau FK, Carpentieri A, De Castro C, Molinaro A, Deho G, Silhavy TJ, Polissi A. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J Bacteriol. 2008 Jul;190(13):4460-9. Epub 2008 Apr 18. PMID:18424520 doi:JB.00270-08
↑ Chng SS, Ruiz N, Chimalakonda G, Silhavy TJ, Kahne D. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. Proc Natl Acad Sci U S A. 2010 Mar 23;107(12):5363-8. doi:, 10.1073/pnas.0912872107. Epub 2010 Mar 4. PMID:20203010 doi:http://dx.doi.org/10.1073/pnas.0912872107
↑ Haarmann R, Ibrahim M, Stevanovic M, Bredemeier R, Schleiff E. The properties of the outer membrane localized Lipid A transporter LptD. J Phys Condens Matter. 2010 Nov 17;22(45):454124. doi:, 10.1088/0953-8984/22/45/454124. Epub 2010 Oct 29. PMID:21339611 doi:http://dx.doi.org/10.1088/0953-8984/22/45/454124
↑ Sampson BA, Misra R, Benson SA. Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability. Genetics. 1989 Jul;122(3):491-501. PMID:2547691
↑ Aono R, Negishi T, Nakajima H. Cloning of organic solvent tolerance gene ostA that determines n-hexane tolerance level in Escherichia coli. Appl Environ Microbiol. 1994 Dec;60(12):4624-6. PMID:7811102
↑ Gennaris A, Nguyen VS, Thouvenel L, Csoma N, Vertommen D, Iorga BI, Remaut H, Collet JF. Optimal functioning of the Lpt bridge depends on a ternary complex between the lipocalin YedD and the LptDE translocon. Cell Rep. 2025 Mar 23;44(4):115446. PMID:40127101 doi:10.1016/j.celrep.2025.115446

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/9fz5"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9fz5 is ON HOLD  until Paper Publication
+==Cryo-EM structure of LptDE-YedD complex from Escherichia Coli==
+<StructureSection load='9fz5' size='340' side='right'caption='[[9fz5]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9fz5]] is a 3 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=9FZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FZ5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.57&#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=9fz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fz5 OCA], [https://pdbe.org/9fz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fz5 RCSB], [https://www.ebi.ac.uk/pdbsum/9fz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fz5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LPTD_ECOLI LPTD_ECOLI] Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance.[HAMAP-Rule:MF_01411]<ref>PMID:12207697</ref> <ref>PMID:12724388</ref> <ref>PMID:16861298</ref> <ref>PMID:18424520</ref> <ref>PMID:20203010</ref> <ref>PMID:21339611</ref> <ref>PMID:2547691</ref> <ref>PMID:7811102</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The outer membrane is an efficient permeability barrier that protects gram-negative bacteria against external assaults, including many antibiotics. The unique permeability features of the outer membrane are due to the presence of lipopolysaccharide (LPS) molecules in its outer leaflet. LPS transport relies on the essential lipopolysaccharide transport (Lpt) pathway, which forms a bridge from the inner to the outer membrane. The LptDE translocon inserts LPS into the outer leaflet. Here, we identify the lipocalin YedD as a component of the translocon. Cryoelectron microscopy of the YedD-LptDE complex reveals that YedD binds LptD at a critical interface between its beta-barrel and periplasmic beta-taco domain. The YedD-LptDE complex is functionally relevant: under conditions where the connectivity of the beta-taco and Lpt bridge is compromised, the absence of YedD decreases cell viability and causes LPS accumulation in the inner membrane. Our findings establish YedD as an Lpt component required for optimal LPS transport.
-Authors:
+Optimal functioning of the Lpt bridge depends on a ternary complex between the lipocalin YedD and the LptDE translocon.,Gennaris A, Nguyen VS, Thouvenel L, Csoma N, Vertommen D, Iorga BI, Remaut H, Collet JF Cell Rep. 2025 Mar 23;44(4):115446. doi: 10.1016/j.celrep.2025.115446. PMID:40127101<ref>PMID:40127101</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 9fz5" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Collet JF]]
+[[Category: Gennaris A]]
+[[Category: Nguyen VS]]
+[[Category: Remaut H]]
+[[Category: Thouvenel L]]

9fz5

From Proteopedia

Current revision

Cryo-EM structure of LptDE-YedD complex from Escherichia Coli

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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