8PHA

O(S)-methyltransferase from Pleurotus sapidus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.02 Å
  • R-Value Free: 0.212 
  • R-Value Work: 0.171 
  • R-Value Observed: 0.173 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

A Novel O - and S -Methyltransferase from Pleurotus sapidus Is Involved in Flavor Formation.

Brescia, F.F.Korf, L.Essen, L.O.Zorn, H.Ruehl, M.

(2024) J Agric Food Chem 72: 6471-6480

  • DOI: https://doi.org/10.1021/acs.jafc.3c08849
  • Primary Citation of Related Structures:  
    8PHA

  • PubMed Abstract: 

    Increasing consumer aversion to non-natural flavoring substances is prompting a heightened interest in enzymatic processes for flavor production. This includes methylation reactions, which are often performed by using hazardous chemicals. By correlation of aroma profile data and transcriptomic analysis, a novel O -methyltransferase (OMT) catalyzing a respective reaction within the formation of p -anisaldehyde was identified in the mushroom Pleurotus sapidus . Heterologous expression in E. coli followed by purification allowed for further characterization of the enzyme. Besides p -hydroxybenzaldehyde, the proposed precursor of p -anisaldehyde, the enzyme catalyzed the methylation of further hydroxylated aromatic compounds at the meta - and para -position. The K m values determined for p -hydroxybenzaldehyde and S -adenosyl-l-methionine were 80 and 107 μM, respectively. Surprisingly, the studied enzyme enabled the transmethylation of thiol-nucleophiles, as indicated by the formation of 2-methyl-3-(methylthio)furan from 2-methyl-3-furanthiol. Moreover, the enzyme was crystallized at a resolution of 2.0 Å, representing the first published crystal structure of a basidiomycetous OMT.


  • Organizational Affiliation

    Institute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Heinrich-Buff-Ring 17, Giessen 35392, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
O-methyltransferase domain-containing protein
A, B, C, D
479Pleurotus sapidusMutation(s): 0 
Gene Names: PLEOSDRAFT_1114007
UniProt
Find proteins for A0A067NAT9 (Pleurotus ostreatus PC15)
Explore A0A067NAT9 
Go to UniProtKB:  A0A067NAT9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A067NAT9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ORN
Query on ORN

Download Ideal Coordinates CCD File 
G [auth A],
J [auth B]
L-ornithine
C5 H12 N2 O2
AHLPHDHHMVZTML-BYPYZUCNSA-N
BGQ
Query on BGQ

Download Ideal Coordinates CCD File 
F [auth A],
I [auth B]
2-HYDROXY BUTANE-1,4-DIOL
C4 H9 O3
ARXKVVRQIIOZGF-SCSAIBSYSA-N
GOL
Query on GOL

Download Ideal Coordinates CCD File 
E [auth A]
H [auth B]
K [auth C]
L [auth C]
O [auth D]
E [auth A],
H [auth B],
K [auth C],
L [auth C],
O [auth D],
P [auth D]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
NA
Query on NA

Download Ideal Coordinates CCD File 
M [auth C],
N [auth C],
Q [auth D],
R [auth D]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.02 Å
  • R-Value Free: 0.212 
  • R-Value Work: 0.171 
  • R-Value Observed: 0.173 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.363α = 90
b = 109.116β = 90
c = 192.925γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
German Federal Ministry for Education and ResearchGermany031B0307B

Revision History  (Full details and data files)

  • Version 1.0: 2024-03-27
    Type: Initial release
  • Version 1.1: 2024-04-10
    Changes: Database references