5dyq

AbyU L73M L139M

spinqualitylabelsall models 5dyq, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dyq is a 4 chain structure with sequence from Micromonospora maris AB-18-032. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Ligands: EPE, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F4F7G1_MICM1 Publication Abstract from PubMed 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. The Catalytic Mechanism of a Natural Diels-Alderase Revealed in Molecular Detail.,Byrne MJ, Lees NR, Han LC, van der Kamp MW, Mulholland AJ, Stach JE, Willis CL, Race PR J Am Chem Soc. 2016 May 18;138(19):6095-8. doi: 10.1021/jacs.6b00232. Epub 2016, May 6. PMID:27140661 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA