4K7Q

Crystal Structure of AcrB Complexed with Linezolid at 3.5 Resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.304 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.255 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of AcrB complexed with linezolid at 3.5 Angstrom resolution.

Hung, L.W.Kim, H.B.Murakami, S.Gupta, G.Kim, C.Y.Terwilliger, T.C.

(2013) J Struct Funct Genomics 14: 71-75

  • DOI: https://doi.org/10.1007/s10969-013-9154-x
  • Primary Citation of Related Structures:  
    4K7Q

  • PubMed Abstract: 

    AcrB is an inner membrane resistance-nodulation-cell division efflux pump and is part of the AcrAB-TolC tripartite efflux system. We have determined the crystal structure of AcrB with bound Linezolid at a resolution of 3.5 Å. The structure shows that Linezolid binds to the A385/F386 loops of the symmetric trimer of AcrB. A conformational change of a loop in the bottom of the periplasmic cleft is also observed.


  • Organizational Affiliation

    Los Alamos National Laboratory, Los Alamos, NM 87545, USA. lwhung@lanl.gov


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Acriflavine resistance protein B1,053Escherichia coli K-12Mutation(s): 0 
Gene Names: acrBacrEb0462JW0451
Membrane Entity: Yes 
UniProt
Find proteins for P31224 (Escherichia coli (strain K12))
Explore P31224 
Go to UniProtKB:  P31224
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP31224
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZLD
Query on ZLD

Download Ideal Coordinates CCD File 
B [auth A]N-{[(5S)-3-(3-fluoro-4-morpholin-4-ylphenyl)-2-oxo-1,3-oxazolidin-5-yl]methyl}acetamide
C16 H20 F N3 O4
TYZROVQLWOKYKF-ZDUSSCGKSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.304 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.255 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 144.685α = 90
b = 144.685β = 90
c = 519.357γ = 120
Software Package:
Software NamePurpose
ADSCdata collection
PHENIXmodel building
PHENIXrefinement
HKL-2000data reduction
SCALEPACKdata scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-07-03
    Type: Initial release
  • Version 1.1: 2015-07-22
    Changes: Non-polymer description
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references, Derived calculations