7V8I

LolCD(E171Q)E with bound AMPPNP in nanodiscs

Summary for 7V8I

• Entry DOI: 10.2210/pdb7v8i/pdb
• EMDB information: 31802
• Descriptor: Lipoprotein-releasing system transmembrane protein LolC, Lipoprotein-releasing system ATP-binding protein LolD, Lipoprotein-releasing system transmembrane protein LolE, ... (5 entities in total)
• Functional Keywords: membrane protein, abc transporter, lipoprotein
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 4
• Total formula weight: 140683.11

Authors

Bei, W.W.,Luo, Q.S.,Shi, H.G.,Zhang, X.Z.,Huang, Y.H. (deposition date: 2021-08-23, release date: 2022-08-31, Last modification date: 2023-10-04)

Primary citation

Bei, W.,Luo, Q.,Shi, H.,Zhou, H.,Zhou, M.,Zhang, X.,Huang, Y.
Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli.
Plos Biol., 20:e3001823-e3001823, 2022

PubMed Abstract: Bacterial lipoproteins perform a diverse array of functions including bacterial envelope biogenesis and microbe-host interactions. Lipoproteins in gram-negative bacteria are sorted to the outer membrane (OM) via the localization of lipoproteins (Lol) export pathway. The ATP-binding cassette (ABC) transporter LolCDE initiates the Lol pathway by selectively extracting and transporting lipoproteins for trafficking. Here, we report cryo-EM structures of LolCDE in apo, lipoprotein-bound, and AMPPNP-bound states at a resolution of 3.5 to 4.2 Å. Structure-based disulfide crosslinking, photo-crosslinking, and functional complementation assay verify the apo-state structure and reveal the molecular details regarding substrate selectivity and substrate entry route. Our studies snapshot 3 functional states of LolCDE in a transport cycle, providing deep insights into the mechanisms that underlie LolCDE-mediated lipoprotein sorting in E. coli.

PubMed: 36228045
DOI: 10.1371/journal.pbio.3001823

Experimental method

ELECTRON MICROSCOPY (3.6 Å)