7cys | pdb_00007cys
Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily
Structural highlights
FunctionAGCT1_HORVU Involved in the synthesis of hordatines (antifungal hydroxycinnamoylagmatine derivatives). Specific for agmatine as the acyl acceptor, inactive towards tyramine and putrescine. Has activity with the acyl donors 4-coumaroyl-CoA, cinnamoyl-CoA, caffeoyl-CoA, feruloyl-CoA, and to a lesser extent sinapoyl-CoA.[1] [2] Publication Abstract from PubMedThe enzymes of the BAHD superfamily, a large group of acyl-CoA-dependent acyltransferases in plants, are involved in the biosynthesis of diverse secondary metabolites. While the structures of several O-acyltransferases from the BAHD superfamily, such as hydroxycinnamoyl-CoA shikimate hydroxycinnamoyl transferase, have been elucidated, no structural information on N-acyltransferases is available. Hordeum vulgare agmatine coumaroyltransferase (HvACT) is an N-acyltransferase from the BAHD superfamily and is one of the most important enzymes in the secondary metabolism of barley. Here, an apo-form structure of HvACT is reported as the first structure of an N-acyltransferase from the BAHD superfamily. HvACT crystals diffracted to 1.8 A resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 57.6, b = 59.5, c = 73.6 A, alpha = 90, beta = 91.3 , gamma = 90 degrees . Like other known BAHD superfamily structures, HvACT contains two domains that adopt a two-layer alphabeta-sandwich architecture and a solvent-exposed channel that penetrates the enzyme core. Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily.,Yamane M, Takenoya M, Yajima S, Sue M Acta Crystallogr F Struct Biol Commun. 2020 Dec 1;76(Pt 12):590-596. doi:, 10.1107/S2053230X20014880. Epub 2020 Nov 25. PMID:33263570[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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