7CYS

Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily

7CYS の概要

• エントリーDOI: 10.2210/pdb7cys/pdb
• 分子名称: Agmatine coumaroyltransferase-1 (2 entities in total)
• 機能のキーワード: acyltransferase, transferase
• 由来する生物種: Hordeum vulgare (Barley)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51628.31

構造登録者

Yamane, M.,Takenoya, M.,Sue, M.,Yajima, S. (登録日: 2020-09-04, 公開日: 2020-12-16, 最終更新日: 2024-10-30)

主引用文献

Yamane, M.,Takenoya, M.,Yajima, S.,Sue, M.
Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily.
Acta Crystallogr.,Sect.F, 76:590-596, 2020

PubMed Abstract: 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 P2, 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.

PubMed: 33263570
DOI: 10.1107/S2053230X20014880

実験手法

X-RAY DIFFRACTION (1.81 Å)