2GFP

Structure of the Multidrug Transporter EmrD from Escherichia coli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.350 
  • R-Value Work: 0.270 
  • R-Value Observed: 0.280 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the multidrug transporter EmrD from Escherichia coli

Yin, Y.He, X.Szewczyk, P.Nguyen, T.Chang, G.

(2006) Science 312: 741-744

  • DOI: https://doi.org/10.1126/science.1125629
  • Primary Citation of Related Structures:  
    2GFP

  • PubMed Abstract: 

    EmrD is a multidrug transporter from the Major Facilitator Superfamily that expels amphipathic compounds across the inner membrane of Escherichia coli. Here, we report the x-ray structure of EmrD determined to a resolution of 3.5 angstroms. The structure reveals an interior that is composed mostly of hydrophobic residues, which is consistent with its role transporting amphipathic molecules. Two long loops extend into the inner leaflet side of the cell membrane. This region can serve to recognize and bind substrate directly from the lipid bilayer. We propose that multisubstrate specificity, binding, and transport are facilitated by these loop regions and the internal cavity.


  • Organizational Affiliation

    Scripps Research Institute, Department of Molecular Biology, 10550 North Torrey Pines Road, CB-105, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Multidrug resistance protein D
A, B
375Escherichia coliMutation(s): 0 
Gene Names: emrD
Membrane Entity: Yes 
UniProt
Find proteins for P31442 (Escherichia coli (strain K12))
Explore P31442 
Go to UniProtKB:  P31442
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP31442
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.350 
  • R-Value Work: 0.270 
  • R-Value Observed: 0.280 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 137.5α = 90
b = 124.5β = 110.2
c = 109.4γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
HKL-2000data reduction
PHASESphasing
X-PLORrefinement
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-05-16
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references