6CHJ

Wax ester synthase/diacylglycerol acyltransferase from Marinobacter aquaeolei VT8


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.43 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.215 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.

Petronikolou, N.Nair, S.K.

(2018) ACS Catal 8: 6334-6344

  • DOI: https://doi.org/10.1021/acscatal.8b00787
  • Primary Citation of Related Structures:  
    6CHJ

  • PubMed Abstract: 

    Wax esters are high-value products whose enzymatic synthesis is of increasing biotechnological interest. The fabrication of cell factories that mass-produce wax esters may provide a facile route towards a sustainable, and environment-friendly approach to a large-scale process for this commodity chemical. An expedient route for wax-ester biocatalysis may be facilitated by the action of enzymes termed wax ester synthases/diacylglycerol acyltransferases (WS/DGAT), which produce wax esters using fatty acids and alcohols as a precursor. In this work, we report the structure for a member of the WS/DGAT superfamily. The structural data in conjunction with bioinformatics and mutational analyses allowed us to identify the substrate binding pockets, and residues that may be important for catalysis. Using this information as a guide, we generated a mutant with preference towards shorter acyl-substrates. This study demonstrates the efficacy of a structure-guided engineering effort towards a WS/DGAT variant with preference towards wax esters of desired lengths.


  • Organizational Affiliation

    Department of Biochemistry, University of Illinois at Urbana Champaign, 600 S. Mathews Ave, Urbana IL USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Diacylglycerol O-acyltransferase
A, B
455Marinobacter nauticus VT8Mutation(s): 0 
Gene Names: Maqu_0168
EC: 2.3.1.20
UniProt
Find proteins for A1TX06 (Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8))
Explore A1TX06 
Go to UniProtKB:  A1TX06
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA1TX06
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.43 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.215 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.268α = 90
b = 103.905β = 103.51
c = 69.529γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
autoPROCdata scaling
PHASERphasing
autoPROCdata processing
autoPROCdata reduction
autoPROCdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-06-13
    Type: Initial release
  • Version 1.1: 2019-10-09
    Changes: Data collection, Database references
  • Version 1.2: 2024-03-06
    Changes: Data collection, Database references, Refinement description
  • Version 1.3: 2024-04-03
    Changes: Refinement description