7z6x

From Proteopedia

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Current revision

Complex of E. coli LolA R43L mutant and lipoprotein

Structural highlights

7z6x is a 1 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 2.06Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LOLA_ECOLI Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.^[1] May act as a regulator of the RCS-phosphorelay signal transduction pathway.^[2]

Publication Abstract from PubMed

In gram-negative bacteria, lipoproteins are vital structural components of the outer membrane (OM) and crucial elements of machineries central to the physiology of the cell envelope. A dedicated apparatus, the Lol system, is required for the correct localization of OM lipoproteins and is essential for viability. The periplasmic chaperone LolA is central to this trafficking pathway, accepting triacylated lipoproteins from the inner membrane transporter LolCDE, before carrying them across the periplasm to the OM receptor LolB. Here, we report a crystal structure of liganded LolA, generated in vivo, revealing the molecular details of lipoprotein association. The structure highlights how LolA, initially primed to receive lipoprotein by interaction with LolC, further opens to accommodate the three ligand acyl chains in a precise conformation within its cavity. LolA forms extensive interactions with the acyl chains but not with any residue of the cargo, explaining the chaperone's ability to transport structurally diverse lipoproteins. Structural characterization of a ligandedLolA variant incapable of lipoprotein release reveals aberrant association, demonstrating the importance of the LolCDE-coordinated, sequential opening of LolA for inserting lipoprotein in a manner productive for subsequent trafficking. Comparison with existing structures of LolA in complex with LolC or LolCDE reveals substantial overlap of the lipoprotein and LolC binding sites within the LolA cavity, demonstrating that insertion of lipoprotein acyl chains physically disengages the chaperone protein from the transporter by perturbing interaction with LolC. Taken together, our data provide a key step toward a complete understanding of a fundamentally important trafficking pathway.

Structural basis of lipoprotein recognition by the bacterial Lol trafficking chaperone LolA.,Kaplan E, Greene NP, Jepson AE, Koronakis V Proc Natl Acad Sci U S A. 2022 Sep 6;119(36):e2208662119. doi:, 10.1073/pnas.2208662119. Epub 2022 Aug 29. PMID:36037338^[3]

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

References

↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
↑ Kaplan E, Greene NP, Jepson AE, Koronakis V. Structural basis of lipoprotein recognition by the bacterial Lol trafficking chaperone LolA. Proc Natl Acad Sci U S A. 2022 Sep 6;119(36):e2208662119. doi:, 10.1073/pnas.2208662119. Epub 2022 Aug 29. PMID:36037338 doi:http://dx.doi.org/10.1073/pnas.2208662119

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/7z6x"

Categories: Escherichia coli K-12 | Large Structures | Greene NP | Kaplan E | Koronakis V

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7z6x]] is a 1 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=7Z6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z6X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IG7:[(2~{S})-3-[(2~{S})-3-azanyl-2-(hexadecanoylamino)-3-oxidanylidene-propyl]sulfanyl-2-hexadecanoyloxy-propyl]+hexadecanoate'>IG7</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IG7:[(2~{S})-3-[(2~{S})-3-azanyl-2-(hexadecanoylamino)-3-oxidanylidene-propyl]sulfanyl-2-hexadecanoyloxy-propyl]+hexadecanoate'>IG7</scene></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=7z6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z6x OCA], [https://pdbe.org/7z6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z6x RCSB], [https://www.ebi.ac.uk/pdbsum/7z6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z6x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/LOLA_ECOLI LOLA_ECOLI]] Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.<ref>PMID:11758943</ref>   May act as a regulator of the RCS-phosphorelay signal transduction pathway.<ref>PMID:11758943</ref>
+[https://www.uniprot.org/uniprot/LOLA_ECOLI LOLA_ECOLI] Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.<ref>PMID:11758943</ref>   May act as a regulator of the RCS-phosphorelay signal transduction pathway.<ref>PMID:11758943</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

7z6x

From Proteopedia

Current revision

Complex of E. coli LolA R43L mutant and lipoprotein

Structural highlights

Function

Publication Abstract from PubMed

References

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