5EIX

QUINOLONE-STABILIZED CLEAVAGE COMPLEX OF TOPOISOMERASE IV FROM KLEBSIELLA PNEUMONIAE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.224 
  • R-Value Observed: 0.226 

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This is version 1.3 of the entry. See complete history


Literature

Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex.

Veselkov, D.A.Laponogov, I.Pan, X.S.Selvarajah, J.Skamrova, G.B.Branstrom, A.Narasimhan, J.Prasad, J.V.Fisher, L.M.Sanderson, M.R.

(2016) Acta Crystallogr D Struct Biol 72: 488-496

  • DOI: https://doi.org/10.1107/S2059798316001212
  • Primary Citation of Related Structures:  
    3RAE, 5EIX

  • PubMed Abstract: 

    Klebsiella pneumoniae is a Gram-negative bacterium that is responsible for a range of common infections, including pulmonary pneumonia, bloodstream infections and meningitis. Certain strains of Klebsiella have become highly resistant to antibiotics. Despite the vast amount of research carried out on this class of bacteria, the molecular structure of its topoisomerase IV, a type II topoisomerase essential for catalysing chromosomal segregation, had remained unknown. In this paper, the structure of its DNA-cleavage complex is reported at 3.35 Å resolution. The complex is comprised of ParC breakage-reunion and ParE TOPRIM domains of K. pneumoniae topoisomerase IV with DNA stabilized by levofloxacin, a broad-spectrum fluoroquinolone antimicrobial agent. This complex is compared with a similar complex from Streptococcus pneumoniae, which has recently been solved.


  • Organizational Affiliation

    Randall Division of Cell and Molecular Biophysics, King's College London, 3rd Floor, New Hunt's House, Guy's Campus, London SE1 1UL, England.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA topoisomerase 4 subunit B,DNA topoisomerase 4 subunit AA,
D [auth B],
G,
J
741Klebsiella pneumoniaeMutation(s): 0 
EC: 5.99.1.3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
SYMMETRISED E-SITE (PRE-CUT)B [auth E],
E [auth C],
H,
K
8synthetic construct
Sequence Annotations
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  • Reference Sequence

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Entity ID: 3
MoleculeChains LengthOrganismImage
SYMMETRISED E-SITE (PRE-CUT)C [auth F],
F [auth D],
I,
L
12synthetic construct
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LFX
Query on LFX

Download Ideal Coordinates CCD File 
O [auth F],
Q [auth D],
T [auth I],
X [auth L]
(3S)-9-fluoro-3-methyl-10-(4-methylpiperazin-1-yl)-7-oxo-2,3-dihydro-7H-[1,4]oxazino[2,3,4-ij]quinoline-6-carboxylic acid
C18 H20 F N3 O4
GSDSWSVVBLHKDQ-JTQLQIEISA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
M [auth A]
N [auth A]
P [auth B]
R [auth G]
S [auth G]
M [auth A],
N [auth A],
P [auth B],
R [auth G],
S [auth G],
U [auth J],
V [auth L],
W [auth L]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.224 
  • R-Value Observed: 0.226 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 102.07α = 90
b = 161.53β = 94.22
c = 138.6γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
PHENIXrefinement

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/K010069/1
PTC fundingUnited Kingdom--

Revision History  (Full details and data files)

  • Version 1.0: 2016-04-13
    Type: Initial release
  • Version 1.1: 2016-05-18
    Changes: Database references
  • Version 1.2: 2017-08-30
    Changes: Author supporting evidence, Derived calculations
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references, Derived calculations