Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.
Journal, issue, pages	Cell, Vol. 169, Issue 2, Page 273-285.e17, Year 2017
Publish date	Apr 6, 2017
Authors	Damian C Ekiert / Gira Bhabha / Georgia L Isom / Garrett Greenan / Sergey Ovchinnikov / Ian R Henderson / Jeffery S Cox / Ronald D Vale /
PubMed Abstract	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) ...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 links	Cell / PubMed:28388411 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.501 - 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 / Water ChemComp-8ND: (2S)-3-(2-aminoethoxy)propane-1,2-diyl dihexadecanoate ChemComp-PEF: DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine
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)
Keywords	TRANSPORT PROTEIN / MCE protein / bacterial lipid transport / phospholipid-binding protein / Lipid-binding / periplasmic / MlaC / transport