4PNE

Crystal Structure of the [4+2]-Cyclase SpnF

Summary for 4PNE

• Entry DOI: 10.2210/pdb4pne/pdb
• Descriptor: Methyltransferase-like protein, S-ADENOSYL-L-HOMOCYSTEINE, MALONATE ION, ... (4 entities in total)
• Functional Keywords: cyclase, sam-dependent methyltransferase-like, spinosyn synthesis, transferase, biosynthetic protein
• Biological source: Saccharopolyspora spinosa
• Total number of polymer chains: 2
• Total formula weight: 66208.64

Authors

Fage, C.D.,Isiorho, E.A.,Liu, Y.-N.,Liu, H.-W.,Keatinge-Clay, A.T. (deposition date: 2014-05-23, release date: 2015-02-18, Last modification date: 2023-09-27)

Primary citation

Fage, C.D.,Isiorho, E.A.,Liu, Y.,Wagner, D.T.,Liu, H.W.,Keatinge-Clay, A.T.
The structure of SpnF, a standalone enzyme that catalyzes [4 + 2] cycloaddition.
Nat.Chem.Biol., 11:256-258, 2015

PubMed Abstract: In the biosynthetic pathway of the spinosyn insecticides, the tailoring enzyme SpnF performs a [4 + 2] cycloaddition on a 22-membered macrolactone to forge an embedded cyclohexene ring. To learn more about this reaction, which could potentially proceed through a Diels-Alder mechanism, we determined the 1.50-Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.

PubMed: 25730549
DOI: 10.1038/nchembio.1768

Experimental method

X-RAY DIFFRACTION (1.5 Å)