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7ARL

LolCDE in complex with lipoprotein and ADP

Summary for 7ARL
Entry DOI10.2210/pdb7arl/pdb
Related7ARH 7ARI 7ARJ 7ARK
EMDB information11886
DescriptorLipoprotein-releasing ABC transporter permease subunit LolC, Lipoprotein-releasing system transmembrane protein LolE, Lipoprotein-releasing system ATP-binding protein LolD, ... (8 entities in total)
Functional Keywordslolcde, lipoprotein, lipoprotein transporter, lipoprotein sorting and transport, protein transport, abc transporter
Biological sourceEscherichia coli (strain K12)
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Total number of polymer chains5
Total formula weight144641.98
Authors
Tang, X.D.,Chang, S.H.,Zhang, K.,Wang, T.,Luo, Q.H.,Qiao, W.,Wang, C.,Shen, C.R.,Zhang, Z.B.,Zhang, Z.Y.,Zhu, X.F.,Wei, X.W.,Dong, C.J.,Zhang, X.,Dong, H.H. (deposition date: 2020-10-25, release date: 2021-04-07, Last modification date: 2024-10-09)
Primary citationTang, 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., 28:347-355, 2021
Cited by
PubMed Abstract: 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 Å, 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.
PubMed: 33782615
DOI: 10.1038/s41594-021-00573-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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건을2024-10-30부터공개중

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