| Autor: |
Yamane M; Department of Agricultural Chemistry, Tokyo University of Agriculture, Sakuragaoka 1-1-1, Setagaya, Tokyo, Japan., Takenoya M; Department of Bioscience, Tokyo University of Agriculture, Sakuragaoka 1-1-1, Setagaya, Tokyo, Japan., Yajima S; Department of Bioscience, Tokyo University of Agriculture, Sakuragaoka 1-1-1, Setagaya, Tokyo, Japan., Sue M; Department of Agricultural Chemistry, Tokyo University of Agriculture, Sakuragaoka 1-1-1, Setagaya, Tokyo, Japan. |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2020 Dec 01; Vol. 76 (Pt 12), pp. 590-596. Date of Electronic Publication: 2020 Nov 25. |
| DOI: |
10.1107/S2053230X20014880 |
| Abstrakt: |
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 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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