7pxo

Structure of the Diels Alderase enzyme AbyU, from Micromonospora maris, co-crystallised with a non transformable substrate analogue

spinqualitylabelsall models 7pxo, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7pxo 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 1.95Å Ligands: 8IF, EPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Diels-Alder reaction is one of the most effective methods for the synthesis of substituted cyclohexenes. The development of protein catalysts for this reaction remains a major priority, affording new sustainable routes to high value target molecules. Whilst a small number of natural enzymes have been shown capable of catalysing [4 + 2] cycloadditions, there is a need for significant mechanistic understanding of how these prospective Diels-Alderases promote catalysis to underpin their development as biocatalysts for use in synthesis. Here we present a molecular description of the complete reaction cycle of the bona fide natural Diels-Alderase AbyU, which catalyses formation of the spirotetronate skeleton of the antibiotic abyssomicin C. This description is derived from X-ray crystallographic studies of AbyU in complex with a non-transformable synthetic substrate analogue, together with transient kinetic analyses of the AbyU catalysed reaction and computational reaction simulations. These studies reveal the mechanistic intricacies of this enzyme system and establish a foundation for the informed reengineering of AbyU and related biocatalysts. Delineation of the complete reaction cycle of a natural Diels-Alderase.,Maschio L, Back CR, Alnawah J, Bowen JI, Johns ST, Mbatha SZ, Han LC, Lees NR, Zorn K, Stach JEM, Hayes MA, van der Kamp MW, Pudney CR, Burston SG, Willis CL, Race PR Chem Sci. 2024 Jun 24;15(29):11572-11583. doi: 10.1039/d4sc02908a. eCollection , 2024 Jul 24. PMID:39055018 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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