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Crystal structure of barley agmatine coumaroyltransferase, an N ‐acyltransferase from the BAHD superfamily
Author(s) -
Yamane Miyo,
Takenoya Mihoko,
Yajima Shunsuke,
Sue Masayuki
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20014880
Subject(s) - acyltransferases , acyltransferase , agmatine , transferase , superfamily , enzyme , biochemistry , chemistry , biosynthesis , biology , gene , putrescine
The 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 Å resolution and belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 57.6, b = 59.5, c = 73.6 Å, α = 90, β = 91.3 , γ = 90°. Like other known BAHD superfamily structures, HvACT contains two domains that adopt a two‐layer αβ‐sandwich architecture and a solvent‐exposed channel that penetrates the enzyme core.