5FN0

Crystal structure of Pseudomonas fluorescens kynurenine-3- monooxygenase (KMO) in complex with GSK180


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.19 Å
  • R-Value Free: 0.196 
  • R-Value Work: 0.157 
  • R-Value Observed: 0.159 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Kynurenine-3-Monooxygenase Inhibition Prevents Multiple Organ Failure in Rodent Models of Acute Pancreatitis.

Mole, D.J.Webster, S.P.Uings, I.Zheng, X.Binnie, M.Wilson, K.Hutchinson, J.P.Mirguet, O.Walker, A.Beaufils, B.Ancellin, N.Trottet, L.Beneton, V.Mowat, C.G.Wilkinson, M.Rowland, P.Haslam, C.Mcbride, A.Homer, N.Z.Baily, J.E.Sharp, M.G.Garden, O.J.Hughes, J.Howie, S.E.Holmes, D.S.Liddle, J.Iredale, J.P.

(2016) Nat Med 22: 202

  • DOI: https://doi.org/10.1038/nm.4020
  • Primary Citation of Related Structures:  
    5FN0

  • PubMed Abstract: 

    Acute pancreatitis (AP) is a common and devastating inflammatory condition of the pancreas that is considered to be a paradigm of sterile inflammation leading to systemic multiple organ dysfunction syndrome (MODS) and death. Acute mortality from AP-MODS exceeds 20% (ref. 3), and the lifespans of those who survive the initial episode are typically shorter than those of the general population. There are no specific therapies available to protect individuals from AP-MODS. Here we show that kynurenine-3-monooxygenase (KMO), a key enzyme of tryptophan metabolism, is central to the pathogenesis of AP-MODS. We created a mouse strain that is deficient for Kmo (encoding KMO) and that has a robust biochemical phenotype that protects against extrapancreatic tissue injury to the lung, kidney and liver in experimental AP-MODS. A medicinal chemistry strategy based on modifications of the kynurenine substrate led to the discovery of the oxazolidinone GSK180 as a potent and specific inhibitor of KMO. The binding mode of the inhibitor in the active site was confirmed by X-ray co-crystallography at 3.2 Å resolution. Treatment with GSK180 resulted in rapid changes in the levels of kynurenine pathway metabolites in vivo, and it afforded therapeutic protection against MODS in a rat model of AP. Our findings establish KMO inhibition as a novel therapeutic strategy in the treatment of AP-MODS, and they open up a new area for drug discovery in critical illness.


  • Organizational Affiliation

    Medical Research Council Centre for Inflammation Research, University of Edinburgh, Edinburgh, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
KYNURENINE 3-MONOOXYGENASE
A, B, C, D
461Pseudomonas fluorescensMutation(s): 2 
EC: 1.14.13.9
UniProt
Find proteins for Q84HF5 (Pseudomonas fluorescens)
Explore Q84HF5 
Go to UniProtKB:  Q84HF5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ84HF5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.19 Å
  • R-Value Free: 0.196 
  • R-Value Work: 0.157 
  • R-Value Observed: 0.159 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 186.85α = 90
b = 105.29β = 90
c = 133.64γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
Aimlessdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2016-01-13
    Type: Initial release
  • Version 1.1: 2016-01-20
    Changes: Database references
  • Version 1.2: 2016-03-02
    Changes: Database references
  • Version 1.3: 2019-05-08
    Changes: Data collection, Experimental preparation, Other