4Z43

Crystal structure of Tryptophan 7-halogenase (PrnA) Mutant E450K


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.29 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.187 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Extending the biocatalytic scope of regiocomplementary flavin-dependent halogenase enzymes.

Shepherd, S.A.Karthikeyan, C.Latham, J.Struck, A.W.Thompson, M.L.Menon, B.R.K.Styles, M.Q.Levy, C.Leys, D.Micklefield, J.

(2015) Chem Sci 6: 3454-3460

  • DOI: https://doi.org/10.1039/c5sc00913h
  • Primary Citation of Related Structures:  
    4Z43, 4Z44

  • PubMed Abstract: 

    Flavin-dependent halogenases are potentially valuable biocatalysts for the regioselective halogenation of aromatic compounds. These enzymes, utilising benign inorganic halides, offer potential advantages over traditional non-enzymatic halogenation chemistry that often lacks regiocontrol and requires deleterious reagents. Here we extend the biocatalytic repertoire of the tryptophan halogenases, demonstrating how these enzymes can halogenate a range of alternative aryl substrates. Using structure guided mutagenesis we also show that it is possible to alter the regioselectivity as well as increase the activity of the halogenases with non-native substrates including anthranilic acid; an important intermediate in the synthesis and biosynthesis of pharmaceuticals and other valuable products.


  • Organizational Affiliation

    School of Chemistry , The University of Manchester , 131 Princess Street , Manchester , M1 7DN , UK . Email: [email protected].


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Flavin-dependent tryptophan halogenase PrnA538Pseudomonas fluorescensMutation(s): 1 
Gene Names: prnA
EC: 1.14.19.9
UniProt
Find proteins for P95480 (Pseudomonas fluorescens)
Explore P95480 
Go to UniProtKB:  P95480
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP95480
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.29 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.187 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 68.74α = 90
b = 68.74β = 90
c = 276.17γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
xia2data reduction
xia2data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

  • Released Date: 2016-01-20 
  • Deposition Author(s): Levy, C.W.

Revision History  (Full details and data files)

  • Version 1.0: 2016-01-20
    Type: Initial release
  • Version 1.1: 2017-05-10
    Changes: Database references
  • Version 1.2: 2018-04-18
    Changes: Data collection, Database references
  • Version 1.3: 2024-01-10
    Changes: Data collection, Database references, Refinement description