|Entry||Database: EMDB / ID: 8608|
|Title||Structure of E. coli MCE protein PqiB, periplasmic domain|
|Map data||E. coli MCE protein PqiB, periplasmic domain|
|Sample||homo hexamer of PqiB|
|Function/homology||Mce/MlaD / MlaD protein / outer membrane-bounded periplasmic space / integral component of membrane / plasma membrane / Paraquat-inducible protein B|
Function and homology information
|Source||Escherichia coli / / bacteria /|
|Method||Cryo EM / single particle reconstruction / 3.96 Å resolution|
|Authors||Bhabha G / Ekiert DC|
|Citation||Journal: Cell / Year: 2017|
Title: Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.
Authors: Damian C Ekiert / Gira Bhabha / Georgia L Isom / Garrett Greenan / Sergey Ovchinnikov / Ian R Henderson / Jeffery S Cox / Ronald D Vale
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.
Copyright: 2017 Elsevier Inc. All rights reserved.
|Validation Report||PDB-ID: 5uvn|
SummaryFull reportAbout validation report
|Date||Deposition: Feb 20, 2017 / Header (metadata) release: Apr 12, 2017 / Map release: Apr 12, 2017 / Last update: Sep 27, 2017|
Downloads & links
|File||emd_8608.map.gz (map file in CCP4 format, 32001 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 1.31 Å|
CCP4 map header:
-Entire homo hexamer of PqiB
|Entire||Name: homo hexamer of PqiB / Number of components: 2|
|Mass||Theoretical: 347 kDa|
-Component #1: protein, homo hexamer of PqiB
|Protein||Name: homo hexamer of PqiB / Recombinant expression: No|
|Mass||Theoretical: 347 kDa|
|Source||Species: Escherichia coli / / bacteria / / Strain: K12|
|Source (engineered)||Expression System: Escherichia coli / / bacteria /|
-Component #2: protein, Paraquat-inducible protein B
|Protein||Name: Paraquat-inducible protein B / Recombinant expression: No|
|Mass||Theoretical: 48.857043 kDa|
|Source (engineered)||Expression System: Escherichia coli / / bacteria / / Strain: K12|
|Specimen||Specimen state: particle / Method: Cryo EM|
|Sample solution||Buffer solution: 20 mM Tris pH 8.0 and 150 mM NaCl / pH: 8|
|Vitrification||Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 80 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 (4k x 4k)|
|Image acquisition||Details: 80 e/A2 is total dose for 50 frames|
|Processing||Method: single particle reconstruction / Applied symmetry: C6 (6 fold cyclic) / Number of projections: 36591|
|3D reconstruction||Software: RELION / Resolution: 3.96 Å / Resolution method: FSC 0.143 CUT-OFF|
|FSC plot (resolution assessment)|
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