7ARJ
LolCDE in complex with lipoprotein and AMPPNP complex undimerized form
Summary for 7ARJ
Entry DOI | 10.2210/pdb7arj/pdb |
Related | 7ARH 7ARI |
EMDB information | 11884 |
Descriptor | Lipoprotein-releasing ABC transporter permease subunit LolC, Lipoprotein-releasing system transmembrane protein LolE, Lipoprotein-releasing system ATP-binding protein LolD, ... (8 entities in total) |
Functional Keywords | lolcde, lipoprotein, lipoprotein transporter, lipoprotein sorting and transport, protein transport |
Biological source | Escherichia coli (strain K12) More |
Total number of polymer chains | 5 |
Total formula weight | 144799.97 |
Authors | Tang, X.D.,Chang, S.H.,Zhang, K.,Wang, T.,Luo, Q.H.,Qiao, W.,Wang, C.,Zhang, Z.B.,Zhang, Z.Y.,Zhu, X.F.,Dong, C.J.,Zhang, X.,Dong, H.H. (deposition date: 2020-10-25, release date: 2021-04-07, Last modification date: 2024-10-23) |
Primary citation | 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., 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: 33782615DOI: 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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