5F2K

Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and octanoate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.

Petronikolou, N.Nair, S.K.

(2015) Chem Biol 22: 1480-1490

  • DOI: https://doi.org/10.1016/j.chembiol.2015.09.011
  • Primary Citation of Related Structures:  
    5F2K, 5F2N, 5F2O

  • PubMed Abstract: 

    Transesterification of fatty acids yields the essential component of biodiesel, but current processes are cost-prohibitive and generate waste. Recent efforts make use of biocatalysts that are effective in diverting products from primary metabolism to yield fatty acid methyl esters in bacteria. These biotransformations require the fatty acid O-methyltransferase (FAMT) from Mycobacterium marinum (MmFAMT). Although this activity was first reported in the literature in 1970, the FAMTs have yet to be biochemically characterized. Here, we describe several crystal structures of MmFAMT, which highlight an unexpected structural conservation with methyltransferases that are involved in plant natural product metabolism. The determinants for ligand recognition are analyzed by kinetic analysis of structure-based active-site variants. These studies reveal how an architectural fold employed in plant natural product biosynthesis is used in bacterial fatty acid O-methylation.


  • Organizational Affiliation

    Department of Biochemistry, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA; Institute for Genomic Biology, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
fatty acid O-methyltransferase
A, B
368Mycobacterium marinum MMutation(s): 0 
Gene Names: MMAR_3356
UniProt
Find proteins for B2HHT4 (Mycobacterium marinum (strain ATCC BAA-535 / M))
Explore B2HHT4 
Go to UniProtKB:  B2HHT4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB2HHT4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.074α = 90
b = 66.131β = 107.36
c = 98.086γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data scaling
PHENIXmodel building
ARPmodel building
Cootmodel building
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-12-30
    Type: Initial release
  • Version 1.1: 2017-11-22
    Changes: Derived calculations, Refinement description
  • Version 1.2: 2024-03-06
    Changes: Data collection, Database references