7CYS

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

Summary for 7CYS

• Entry DOI: 10.2210/pdb7cys/pdb
• Descriptor: Agmatine coumaroyltransferase-1 (2 entities in total)
• Functional Keywords: acyltransferase, transferase
• Biological source: Hordeum vulgare (Barley)
• Total number of polymer chains: 1
• Total formula weight: 51628.31

Authors

Yamane, M.,Takenoya, M.,Sue, M.,Yajima, S. (deposition date: 2020-09-04, release date: 2020-12-16, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.81 Å)