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TitleArchitectures of Lipid Transport Systems for the Bacterial Outer Membrane.
Journal, issue, pagesCell, Vol. 169, Issue 2, Page 273-285.e17, Year 2017
Publish dateApr 6, 2017
AuthorsDamian C Ekiert / Gira Bhabha / Georgia L Isom / Garrett Greenan / Sergey Ovchinnikov / Ian R Henderson / Jeffery S Cox / Ronald D Vale /
PubMed AbstractHow phospholipids are trafficked between the bacterial inner and outer membranes through the hydrophilic space of the periplasm is not known. We report that members of the mammalian cell entry (MCE) ...How phospholipids are trafficked between the bacterial inner and outer membranes through the hydrophilic space of the periplasm is not known. We report that members of the mammalian cell entry (MCE) protein family form hexameric assemblies with a central channel capable of mediating lipid transport. The E. coli MCE protein, MlaD, forms a ring associated with an ABC transporter complex in the inner membrane. A soluble lipid-binding protein, MlaC, ferries lipids between MlaD and an outer membrane protein complex. In contrast, EM structures of two other E. coli MCE proteins show that YebT forms an elongated tube consisting of seven stacked MCE rings, and PqiB adopts a syringe-like architecture. Both YebT and PqiB create channels of sufficient length to span the periplasmic space. This work reveals diverse architectures of highly conserved protein-based channels implicated in the transport of lipids between the membranes of bacteria and some eukaryotic organelles.
External linksCell / PubMed:28388411 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.501 - 25.0 Å
Structure data

8608

5uvn

EMDB-8608, PDB-5uvn:
Structure of E. coli MCE protein PqiB, periplasmic domain
Method: EM (single particle) / Resolution: 3.96 Å

EMDB-8610:
Structure of E. coli MCE protein PqiB, periplasmic domain
Method: EM (single particle) / Resolution: 10.0 Å

EMDB-8611:
Negative stain reconstruction of E. coli MCE protein YebT
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-8612:
Negative stain reconstruction of E. coli MCE protein PqiB
Method: EM (single particle) / Resolution: 25.0 Å

PDB-5uw2:
Structure of E. coli MCE protein MlaD, periplasmic domain
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

PDB-5uw8:
Structure of E. coli MCE protein MlaD, core MCE domain
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-5uwa:
Structure of E. coli phospholipid binding protein MlaC
Method: X-RAY DIFFRACTION / Resolution: 1.501 Å

PDB-5uwb:
Re-refined 4FCZ: lipid-bound crystal structure of toluene-tolerance protein from Pseudomonas putida
Method: X-RAY DIFFRACTION / Resolution: 2.604 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-8ND:
(2S)-3-(2-aminoethoxy)propane-1,2-diyl dihexadecanoate

ChemComp-PEF:
DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • escherichia coli (E. coli)
  • escherichia coli o157:h7 (bacteria)
  • escherichia coli (strain k12) (bacteria)
  • pseudomonas putida (strain atcc 47054 / dsm 6125 / ncimb 11950 / kt2440) (bacteria)
KeywordsTRANSPORT PROTEIN / MCE protein / bacterial lipid transport / phospholipid-binding protein / Lipid-binding / periplasmic / MlaC / transport

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