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TitleDeciphering the molecular basis of lipoprotein recognition and transport by LolCDE.
Journal, issue, pagesSignal Transduct Target Ther, Vol. 9, Issue 1, Page 354, Year 2024
Publish dateDec 27, 2024
AuthorsWen Qiao / Chongrong Shen / Yujiao Chen / Shenghai Chang / Xin Wang / Lili Yang / Jie Pang / Qinghua Luo / Zhibo Zhang / Yingxin Xiang / Chao Zhao / Guangwen Lu / Bi-Sen Ding / Binwu Ying / Xiaodi Tang / Haohao Dong /
PubMed AbstractOuter membrane (OM) lipoproteins serve vital roles in Gram-negative bacteria, contributing to their pathogenicity and drug resistance. For these lipoproteins to function, they must be transported ...Outer membrane (OM) lipoproteins serve vital roles in Gram-negative bacteria, contributing to their pathogenicity and drug resistance. For these lipoproteins to function, they must be transported from the inner membrane (IM), where they are assembled, to the OM by the ABC transporter LolCDE. We have previously captured structural snapshots of LolCDE in multiple states, revealing its dynamic conformational changes. However, the exact mechanism by which LolCDE recognizes and transfers lipoprotein between domains remains unclear. Here, we characterized the E. coli LolCDE complex bound with endogenous lipoprotein or ATP to explore the molecular features governing its substrate binding and transport functions. We found that the N-terminal unstructured linker of lipoprotein is critical for efficient binding by LolCDE; it must be sufficiently long to keep the lipoprotein's main body outside the complex while allowing the triacyl chains to bind within the central cavity. Mutagenic assays identified key residues that mediate allosteric communication between the cytoplasmic and transmembrane domains and in the periplasmic domain to form a lipoprotein transport pathway at the LolC-LolE interface. This study provides insights into the OM lipoprotein relocation process mediated by LolCDE, with significant implications for antimicrobial drug development.
External linksSignal Transduct Target Ther / PubMed:39725716 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

51520

9grc

EMDB-51520, PDB-9grc:
Cryo-EM structure of lipoprotein-bound LolCDE in nanodiscs
Method: EM (single particle) / Resolution: 3.5 Å

51637

9gvk

EMDB-51637, PDB-9gvk:
Cryo-EM structure of endogenous ATP-bound LolCDE with LolD-E171Q mutations in nanodiscs
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-Z41:
(2S)-3-hydroxypropane-1,2-diyl dihexadecanoate

ChemComp-PLM:
PALMITIC ACID

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • escherichia coli k-12 (bacteria)
KeywordsTRANSPORT PROTEIN / LolCDE / /lipoprotein / /extraction / /transportation

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