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• W2107777666 startingPage "2032" @default.
• W2107777666 abstract "Plant 4-coumarate:CoA ligase (4CL) serves as a central catalyst in the phenylpropanoid pathway that provides precursors for numerous metabolites and regulates carbon flow. Here, we present several high-resolution crystal structures of Nicotiana tabacum 4CL isoform 2 (Nt4CL2) in complex with Mg(2+) and ATP, with AMP and coenzyme A (CoA), and with three different hydroxycinnamate-AMP intermediates: 4-coumaroyl-AMP, caffeoyl-AMP, and feruloyl-AMP. The Nt4CL2-Mg(2+)-ATP structure is captured in the adenylate-forming conformation, whereas the other structures are in the thioester-forming conformation. These structures represent a rare example of an ANL enzyme visualized in both conformations, and also reveal the binding determinants for both CoA and the hydroxycinnamate substrate. Kinetic studies of structure-based variants were used to identify residues crucial to catalysis, ATP binding, and hydroxycinnamate specificity. Lastly, we characterize a deletion mutant of Nt4CL2 that possesses the unusual sinapinate-utilizing activity. These studies establish a molecular framework for the engineering of this versatile biocatalyst." @default.
• W2107777666 created "2016-06-24" @default.
• W2107777666 creator A5025967890 @default.
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• W2107777666 date "2015-11-01" @default.
• W2107777666 modified "2023-10-14" @default.
• W2107777666 title "Structural Basis for Specificity and Flexibility in a Plant 4-Coumarate:CoA Ligase" @default.
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• W2107777666 doi "https://doi.org/10.1016/j.str.2015.08.012" @default.
• W2107777666 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26412334" @default.
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