6MYW

Gluconobacter Ene-Reductase (GluER) mutant - T36A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.16 Å
  • R-Value Free: 0.145 
  • R-Value Work: 0.123 
  • R-Value Observed: 0.124 

wwPDB Validation   3D Report Full Report

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This is version 1.2 of the entry. See complete history


Literature

Photoexcitation of flavoenzymes enables a stereoselective radical cyclization.

Biegasiewicz, K.F.Cooper, S.J.Gao, X.Oblinsky, D.G.Kim, J.H.Garfinkle, S.E.Joyce, L.A.Sandoval, B.A.Scholes, G.D.Hyster, T.K.

(2019) Science 364: 1166-1169

  • DOI: https://doi.org/10.1126/science.aaw1143
  • Primary Citation of Related Structures:  
    6MYW, 6O08

  • PubMed Abstract: 

    Photoexcitation is a common strategy for initiating radical reactions in chemical synthesis. We found that photoexcitation of flavin-dependent "ene"-reductases changes their catalytic function, enabling these enzymes to promote an asymmetric radical cyclization. This reactivity enables the construction of five-, six-, seven-, and eight-membered lactams with stereochemical preference conferred by the enzyme active site. After formation of a prochiral radical, the enzyme guides the delivery of a hydrogen atom from flavin-a challenging feat for small-molecule chemical reagents. The initial electron transfer occurs through direct excitation of an electron donor-acceptor complex that forms between the substrate and the reduced flavin cofactor within the enzyme active site. Photoexcitation of promiscuous flavoenzymes has thus furnished a previously unknown biocatalytic reaction.


  • Organizational Affiliation

    Department of Chemistry, Princeton University, Princeton, NJ 08544, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
N-ethylmaleimide reductase
A, B, C, D
369Gluconobacter oxydansMutation(s): 1 
Gene Names: noxAD934_01855AD950_09540
UniProt
Find proteins for A1E8I9 (Gluconobacter oxydans)
Explore A1E8I9 
Go to UniProtKB:  A1E8I9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA1E8I9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
FMN
Query on FMN

Download Ideal Coordinates CCD File 
E [auth A],
I [auth B],
O [auth C],
Z [auth D]
FLAVIN MONONUCLEOTIDE
C17 H21 N4 O9 P
FVTCRASFADXXNN-SCRDCRAPSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
BA [auth D]
CA [auth D]
DA [auth D]
G [auth A]
H [auth A]
BA [auth D],
CA [auth D],
DA [auth D],
G [auth A],
H [auth A],
K [auth B],
L [auth B],
Q [auth C],
R [auth C],
S [auth C]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
GOL
Query on GOL

Download Ideal Coordinates CCD File 
Y [auth C]GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
ACT
Query on ACT

Download Ideal Coordinates CCD File 
AA [auth D],
F [auth A],
J [auth B],
P [auth C]
ACETATE ION
C2 H3 O2
QTBSBXVTEAMEQO-UHFFFAOYSA-M
NA
Query on NA

Download Ideal Coordinates CCD File 
M [auth B]
N [auth B]
T [auth C]
U [auth C]
V [auth C]
M [auth B],
N [auth B],
T [auth C],
U [auth C],
V [auth C],
W [auth C],
X [auth C]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.16 Å
  • R-Value Free: 0.145 
  • R-Value Work: 0.123 
  • R-Value Observed: 0.124 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.475α = 90
b = 45.154β = 107.67
c = 163.744γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-06-26
    Type: Initial release
  • Version 1.1: 2019-07-03
    Changes: Data collection, Database references
  • Version 1.2: 2023-10-11
    Changes: Data collection, Database references, Derived calculations, Refinement description