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Structure paper

TitleStructural basis for bacterial lipoprotein relocation by the transporter LolCDE.
Journal, issue, pagesNat Struct Mol Biol, Vol. 28, Issue 4, Page 347-355, Year 2021
Publish dateMar 29, 2021
AuthorsXiaodi Tang / Shenghai Chang / Ke Zhang / Qinghua Luo / Zhengyu Zhang / Ting Wang / Wen Qiao / Chen Wang / Chongrong Shen / Zhibo Zhang / Xiaofeng Zhu / Xiawei Wei / Changjiang Dong / Xing Zhang / Haohao Dong /
PubMed AbstractLipoproteins 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 ...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.
External linksNat Struct Mol Biol / PubMed:33782615
MethodsEM (single particle)
Resolution3.2 - 4.1 Å
Structure data

EMDB-11882, PDB-7arh:
LolCDE in complex with lipoprotein
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-11883, PDB-7ari:
LolCDE apo structure
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-11884, PDB-7arj:
LolCDE in complex with lipoprotein and AMPPNP complex undimerized form
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-11885, PDB-7ark:
LolCDE in complex with AMP-PNP in the closed NBD state
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-11886, PDB-7arl:
LolCDE in complex with lipoprotein and ADP
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-11887, PDB-7arm:
LolCDE in complex with lipoprotein and LolA
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-Z41:
(2S)-3-hydroxypropane-1,2-diyl dihexadecanoate

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • Escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli k-12 (bacteria)
  • escherichia coli bl21(de3) (bacteria)
KeywordsPROTEIN TRANSPORT / LolCDE / lipoprotein / lipoprotein transporter / lipoprotein sorting and transport / ABC transporter

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