5UVN

Structure of E. coli MCE protein PqiB, periplasmic domain

  • Classification: TRANSPORT PROTEIN
  • Organism(s): Escherichia coli K-12
  • Expression System: Escherichia coli
  • Mutation(s): No 
  • Membrane Protein: Yes  mpstruc

  • Deposited: 2017-02-20 Released: 2017-04-12 
  • Deposition Author(s): Bhabha, G., Ekiert, D.C.
  • Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS), Damon Runyon Cancer Research Foundation, Howard Hughes Medical Institute (HHMI)

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.96 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.

Ekiert, D.C.Bhabha, G.Isom, G.L.Greenan, G.Ovchinnikov, S.Henderson, I.R.Cox, J.S.Vale, R.D.

(2017) Cell 169: 273-285.e17

  • DOI: https://doi.org/10.1016/j.cell.2017.03.019
  • Primary Citation of Related Structures:  
    5UVN, 5UW2, 5UW8, 5UWA, 5UWB

  • 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) 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.


  • Organizational Affiliation

    Department of Cellular and Molecular Pharmacology and the Howard Hughes Medical Institute, The University of California, San Francisco, 600 16(th) Street, San Francisco, CA 94158, USA; Department of Microbiology and Immunology, The University of California, San Francisco, 600 16(th) Street, San Francisco, CA 94158, USA. Electronic address: damian.ekiert@med.nyu.edu.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Paraquat-inducible protein B
A, B, C, D, E
A, B, C, D, E, F
453Escherichia coli K-12Mutation(s): 0 
Gene Names: pqiBpqi5Bb0951JW0934
Membrane Entity: Yes 
UniProt
Find proteins for P43671 (Escherichia coli (strain K12))
Explore P43671 
Go to UniProtKB:  P43671
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43671
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.96 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION1.4
MODEL REFINEMENTPHENIX1.9

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesK99GM112982
Damon Runyon Cancer Research FoundationUnited StatesDRG-2140-12
Howard Hughes Medical Institute (HHMI)United States--

Revision History  (Full details and data files)

  • Version 1.0: 2017-04-12
    Type: Initial release
  • Version 1.1: 2017-04-19
    Changes: Database references
  • Version 1.2: 2017-09-27
    Changes: Author supporting evidence, Data collection
  • Version 1.3: 2018-07-18
    Changes: Data collection, Experimental preparation
  • Version 1.4: 2018-10-03
    Changes: Data collection, Refinement description
  • Version 1.5: 2019-11-20
    Changes: Author supporting evidence
  • Version 1.6: 2024-03-13
    Changes: Data collection, Database references