|Entry||Database: PDB / ID: 5uvn|
|Title||Structure of E. coli MCE protein PqiB, periplasmic domain|
|Components||Paraquat-inducible protein B|
|Keywords||TRANSPORT PROTEIN / MCE protein / bacterial lipid transport|
|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
|Specimen source||Escherichia coli / bacteria / /|
|Method||Electron microscopy (3.96 Å resolution / Particle / Single particle) / Transmission electron microscopy|
|Authors||Bhabha, G. / Ekiert, D.C.|
|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.
SummaryFull reportAbout validation report
|Date||Deposition: Feb 20, 2017 / Release: Apr 12, 2017|
Downloads & links
A: Paraquat-inducible protein B
B: Paraquat-inducible protein B
C: Paraquat-inducible protein B
D: Paraquat-inducible protein B
E: Paraquat-inducible protein B
F: Paraquat-inducible protein B
Mass: 48857.043 Da / Num. of mol.: 6 / Source: (gene. exp.) Escherichia coli / bacteria / / / Strain: K12 / Gene: pqiB, pqi5B, b0951, JW0934 / Production host: Escherichia coli / References: UniProt:P43671
|Sequence details||The actual sample sequence is MHHHHHHENLYFQSHQGPEVTLITANAEGIEGGKTTIKSRSVDVGVVESATLADD ...The actual sample sequence is MHHHHHHENL|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE|
|Component||Name: homo hexamer of PqiB / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT|
|Molecular weight||Value: 0.347 deg. / Units: MEGADALTONS|
|Source (natural)||Organism: Escherichia coli / Strain: K12|
|Source (recombinant)||Organism: Escherichia coli|
|Buffer solution||Details: 20 mM Tris pH 8.0 and 150 mM NaCl / pH: 8|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER / Grid mesh size: 400 / Grid type: Quantifoil 1.2/1.3|
|Vitrification||Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELD|
|Image recording||Electron dose: 80 e/Å2 / Details: 80 e/A2 is total dose for 50 frames / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|Software||Name: PHENIX / Version: 1.10.1_2155: / Classification: refinement|
|CTF correction||Type: NONE|
|Symmetry||Point symmetry: C6|
|3D reconstruction||Resolution: 3.96 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 36591 / Symmetry type: POINT|
|Atomic model building||Ref protocol: OTHER / Ref space: REAL|
|Least-squares process||Highest resolution: 3.96 Å|
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