5F2K

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

Summary for 5F2K

• Entry DOI: 10.2210/pdb5f2k/pdb
• Related: 5F2N 5F2O
• Descriptor: fatty acid O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, OCTANOIC ACID (CAPRYLIC ACID), ... (4 entities in total)
• Functional Keywords: fatty acid methyltransferase, octanoate, methyltransferase, transferase
• Biological source: Mycobacterium marinum (strain ATCC BAA-535 / M)
• Total number of polymer chains: 2
• Total formula weight: 81730.27

Authors

Petronikolou, N.,Nair, S.K. (deposition date: 2015-12-02, release date: 2015-12-30, Last modification date: 2024-03-06)

Primary citation

Petronikolou, N.,Nair, S.K.
Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.
Chem.Biol., 22:1480-1490, 2015

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.

PubMed: 26526103
DOI: 10.1016/j.chembiol.2015.09.011

Experimental method

X-RAY DIFFRACTION (1.6 Å)