Structural highlights
Function
LOLC_ECOLI Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.
Publication Abstract from PubMed
Lipoproteins in the outer membrane of Gram-negative bacteria are involved in various vital physiological activities, including multidrug resistance. Synthesized in the cytoplasm and matured in the inner membrane, lipoproteins must be transported to the outer membrane through the Lol pathway mediated by the ATP-binding cassette transporter LolCDE in the inner membrane via an unknown mechanism. Here, we report cryo-EM structures of Escherichia coli LolCDE in apo, lipoprotein-bound, LolA-bound, ADP-bound and AMP-PNP-bound states at a resolution of 3.2-3.8 A, covering the complete lipoprotein transport cycle. Mutagenesis and in vivo viability assays verify features of the structures and reveal functional residues and structural characteristics of LolCDE. The results provide insights into the mechanisms of sorting and transport of outer-membrane lipoproteins and may guide the development of novel therapies against multidrug-resistant Gram-negative bacteria.
Structural basis for bacterial lipoprotein relocation by the transporter LolCDE.,Tang X, Chang S, Zhang K, Luo Q, Zhang Z, Wang T, Qiao W, Wang C, Shen C, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H Nat Struct Mol Biol. 2021 Apr;28(4):347-355. doi: 10.1038/s41594-021-00573-x. , Epub 2021 Mar 29. PMID:33782615[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tang X, Chang S, Zhang K, Luo Q, Zhang Z, Wang T, Qiao W, Wang C, Shen C, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H. Structural basis for bacterial lipoprotein relocation by the transporter LolCDE. Nat Struct Mol Biol. 2021 Apr;28(4):347-355. PMID:33782615 doi:10.1038/s41594-021-00573-x
