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Crystal structure of barley agmatine coumaroyltransferase, an N‐acyltransferase from the BAHD superfamily
Acta Crystallographica Section F ( IF 1.1 ) Pub Date : 2020-12-04 , DOI: 10.1107/s2053230x20014880
Miyo Yamane 1 , Mihoko Takenoya 2 , Shunsuke Yajima 2 , Masayuki Sue 1
Affiliation  

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 P21, 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.

中文翻译:

大麦丁香豆酰转移酶的晶体结构,一种来自 BAHD 超家族的 N-酰基转移酶

BAHD 超家族的酶是植物中一大群依赖于酰基辅酶 A 的酰基转移酶,参与多种次生代谢物的生物合成。虽然已经阐明了来自 BAHD 超家族的几种O-酰基转移酶的结构,例如羟基肉桂酰基-CoA 莽草酸羟基肉桂酰基转移酶,但没有关于N-酰基转移酶的结构信息。Hordeum vulgare胍丁胺香豆酰转移酶 (HvACT) 是来自 BAHD 超家族的N-酰基转移酶,是大麦次级代谢中最重要的酶之一。在这里,HvACT 的 apo 型结构被报告为N的第一个结构-来自 BAHD 超家族的酰基转移酶。HvACT 晶体衍射到 1.8 Å 分辨率,属于单斜空间群P 2 1,晶胞参数a = 57.6, b = 59.5, c  = 73.6 Å, α = 90, β = 91.3 , γ = 90°。与其他已知的 BAHD 超家族结构一样,HvACT 包含两个结构域,它们采用双层 αβ 夹心结构和一个穿透酶核心的溶剂暴露通道。
更新日期:2020-12-04
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