2XKK

CRYSTAL STRUCTURE OF MOXIFLOXACIN, DNA, and A. BAUMANNII TOPO IV (PARE-PARC FUSION TRUNCATE)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.25 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.197 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Structural Basis of Quinolone Inhibition of Type Iia Topoisomerases and Target-Mediated Resistance

Wohlkonig, A.Chan, P.F.Fosberry, A.P.Homes, P.Huang, J.Kranz, M.Leydon, V.R.Miles, T.J.Pearson, N.D.Perera, R.L.Shillings, A.J.Gwynn, M.N.Bax, B.D.

(2010) Nat Struct Mol Biol 17: 1152

  • DOI: https://doi.org/10.1038/nsmb.1892
  • Primary Citation of Related Structures:  
    2XKJ, 2XKK

  • PubMed Abstract: 

    Quinolone antibacterials have been used to treat bacterial infections for over 40 years. A crystal structure of moxifloxacin in complex with Acinetobacter baumannii topoisomerase IV now shows the wedge-shaped quinolone stacking between base pairs at the DNA cleavage site and binding conserved residues in the DNA cleavage domain through chelation of a noncatalytic magnesium ion. This provides a molecular basis for the quinolone inhibition mechanism, resistance mutations and invariant quinolone antibacterial structural features.


  • Organizational Affiliation

    Platform Technology and Science, GlaxoSmithKline, Medicines Research Centre, Stevenage, Hertfordshire, UK.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TOPOISOMERASE IVA,
B [auth C]
767Acinetobacter baumanniiMutation(s): 0 
EC: 5.99.1
UniProt
Find proteins for B0VP98 (Acinetobacter baumannii (strain SDF))
Explore B0VP98 
Go to UniProtKB:  B0VP98
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB0VP98
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains LengthOrganismImage
DNAC [auth E]34synthetic construct
Sequence Annotations
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  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains LengthOrganismImage
DNAD [auth F]34synthetic construct
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.25 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.197 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 199.775α = 90
b = 95.566β = 108.27
c = 118.092γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKLdata reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2010-09-01
    Type: Initial release
  • Version 1.1: 2011-10-12
    Changes: Database references, Version format compliance
  • Version 1.2: 2023-12-20
    Changes: Advisory, Data collection, Database references, Derived calculations, Other, Refinement description