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TitleRole of Ring6 in the Function of the E. coli MCE Protein LetB.
Journal, issue, pagesJ Mol Biol, Vol. 434, Issue 7, Page 167463, Year 2022
Publish dateApr 15, 2022
AuthorsCasey Vieni / Nicolas Coudray / Georgia L Isom / Gira Bhabha / Damian C Ekiert /
PubMed AbstractLetB is a tunnel-forming protein found in the cell envelope of some double-membraned bacteria, and is thought to be important for the transport of lipids between the inner and outer membranes. In ...LetB is a tunnel-forming protein found in the cell envelope of some double-membraned bacteria, and is thought to be important for the transport of lipids between the inner and outer membranes. In Escherichia coli the LetB tunnel is formed from a stack of seven rings (Ring1 - Ring7), in which each ring is composed of a homo-hexameric assembly of MCE domains. The primary sequence of each MCE domain of the LetB protein is substantially divergent from the others, making each MCE ring unique in nature. The role of each MCE domain and how it contributes to the function of LetB is not well understood. Here we probed the importance of each MCE ring for the function of LetB, using a combination of bacterial growth assays and cryo-EM. Surprisingly, we find that ΔRing3 and ΔRing6 mutants, in which Ring3 and Ring6 have been deleted, confer increased resistance to membrane perturbing agents. Specific mutations in the pore-lining loops of Ring6 similarly confer increased resistance. A cryo-EM structure of the ΔRing6 mutant shows that despite the absence of Ring6, which leads to a shorter assembly, the overall architecture is maintained, highlighting the modular nature of MCE proteins. Previous work has shown that Ring6 is dynamic and in its closed state, may restrict the passage of substrate through the tunnel. Our work suggests that removal of Ring6 may relieve this restriction. The deletion of Ring6 combined with mutations in the pore-lining loops leads to a model for the tunnel gating mechanism of LetB. Together, these results provide insight into the functional roles of individual MCE domains and pore-lining loops in the LetB protein.
External linksJ Mol Biol / PubMed:35077766 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.55 Å
Structure data

25066

7see

EMDB-25066, PDB-7see:
Structure of E. coli LetB delta (Ring6) mutant, Ring1 in the closed state (Model 1)
Method: EM (single particle) / Resolution: 3.2 Å

25067

7sef

EMDB-25067, PDB-7sef:
Structure of E. coli LetB delta (Ring6) mutant, Ring 1 in the open state (Model 2, Rings 1-3 only)
Method: EM (single particle) / Resolution: 3.55 Å

Chemicals

ChemComp-UNX:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsLIPID TRANSPORT / bacterial cell envelope / MCE

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