7ARH

LolCDE in complex with lipoprotein


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

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.

(2021) Nat Struct Mol Biol 28: 347-355

  • DOI: 10.1038/s41594-021-00573-x
  • Primary Citation of Related Structures:  
    7ARI, 7ARH, 7ARK, 7ARJ, 7ARM, 7ARL

  • 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 ...

    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.


    Organizational Affiliation

    State Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, Sichuan, China. haohaodong@scu.edu.cn.



Macromolecules
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Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
Lipoprotein-releasing ABC transporter permease subunit LolCA [auth C]399Escherichia coli K-12Mutation(s): 0 
Gene Names: lolCFAZ83_19940
Membrane protein
Mpstruc
Group: 
TRANSMEMBRANE PROTEINS: ALPHA-HELICAL
Sub Group: 
ATP Binding Cassette (ABC) Transporters
Protein: 
lipoprotein outer membrane localization (Lol) protein LolCDE in complex with lipoprotein
Find proteins for A0A4S5ATA9 (Escherichia coli (strain K12))
Explore A0A4S5ATA9 
Go to UniProtKB:  A0A4S5ATA9
Protein Feature View
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  • Reference Sequence
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Entity ID: 2
MoleculeChainsSequence LengthOrganismDetailsImage
Lipoprotein-releasing system transmembrane protein LolEB [auth E]414Escherichia coli K-12Mutation(s): 0 
Gene Names: lolEycfWb1118JW1104
Membrane protein
Mpstruc
Group: 
TRANSMEMBRANE PROTEINS: ALPHA-HELICAL
Sub Group: 
ATP Binding Cassette (ABC) Transporters
Protein: 
lipoprotein outer membrane localization (Lol) protein LolCDE in complex with lipoprotein
Find proteins for P75958 (Escherichia coli (strain K12))
Explore P75958 
Go to UniProtKB:  P75958
Protein Feature View
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  • Reference Sequence
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Entity ID: 3
MoleculeChainsSequence LengthOrganismDetailsImage
Lipoprotein-releasing system ATP-binding protein LolDD, C [auth F]241Escherichia coli K-12Mutation(s): 0 
Gene Names: lolDycfVb1117JW5162
EC: 7.6.2
Membrane protein
Mpstruc
Group: 
TRANSMEMBRANE PROTEINS: ALPHA-HELICAL
Sub Group: 
ATP Binding Cassette (ABC) Transporters
Protein: 
lipoprotein outer membrane localization (Lol) protein LolCDE in complex with lipoprotein
Find proteins for P75957 (Escherichia coli (strain K12))
Explore P75957 
Go to UniProtKB:  P75957
Protein Feature View
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  • Reference Sequence
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Entity ID: 4
MoleculeChainsSequence LengthOrganismDetailsImage
LPPE [auth V]10Escherichia coli K-12Mutation(s): 0 
Gene Names: LPP
Protein Feature View
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
Z41
Query on Z41

Download Ideal Coordinates CCD File 
F [auth C](2S)-3-hydroxypropane-1,2-diyl dihexadecanoate
C35 H68 O5
JEJLGIQLPYYGEE-XIFFEERXSA-N
 Ligand Interaction
PLM
Query on PLM

Download Ideal Coordinates CCD File 
G [auth V]PALMITIC ACID
C16 H32 O2
IPCSVZSSVZVIGE-UHFFFAOYSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2021-04-07
    Type: Initial release
  • Version 1.1: 2021-04-14
    Changes: Database references
  • Version 1.2: 2021-04-28
    Changes: Database references