5DYQ

AbyU L73M L139M

Summary for 5DYQ

• Entry DOI: 10.2210/pdb5dyq/pdb
• Descriptor: YD repeat-containing protein, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: [4+2] cycloaddition, diels-alderase, diels-alder, tetronate, spirotetronate, polyketide, abyssomicin, ligase
• Biological source: Verrucosispora maris
• Total number of polymer chains: 4
• Total formula weight: 72852.72

Authors

Byrne, M.J.,Race, P.R. (deposition date: 2015-09-25, release date: 2016-06-08, Last modification date: 2024-10-16)

Primary citation

Byrne, M.J.,Lees, N.R.,Han, L.C.,van der Kamp, M.W.,Mulholland, A.J.,Stach, J.E.,Willis, C.L.,Race, P.R.
The Catalytic Mechanism of a Natural Diels-Alderase Revealed in Molecular Detail.
J.Am.Chem.Soc., 138:6095-6098, 2016

PubMed Abstract: The Diels-Alder reaction, a [4 + 2] cycloaddition of a conjugated diene to a dienophile, is one of the most powerful reactions in synthetic chemistry. Biocatalysts capable of unlocking new and efficient Diels-Alder reactions would have major impact. Here we present a molecular-level description of the reaction mechanism of the spirotetronate cyclase AbyU, an enzyme shown here to be a bona fide natural Diels-Alderase. Using enzyme assays, X-ray crystal structures, and simulations of the reaction in the enzyme, we reveal how linear substrate chains are contorted within the AbyU active site to facilitate a transannular pericyclic reaction. This study provides compelling evidence for the existence of a natural enzyme evolved to catalyze a Diels-Alder reaction and shows how catalysis is achieved.

PubMed: 27140661
DOI: 10.1021/jacs.6b00232

Experimental method

X-RAY DIFFRACTION (1.66 Å)