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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Crystal structure of fungal tannase from Aspergillus niger
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Crystal structure of fungal tannase from Aspergillus niger

机译：真菌丹宁酸酶的晶体结构黑曲霉

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摘要

Tannases are serine esterases that were first discovered in fungi more than one and half centuries ago. They catalyze the hydrolysis of the gallolyl ester bonds in gallotannins to release gallic acid, which is an important intermediate in the chemical and pharmaceutical industries. Since their discovery, fungal tannases have found wide industrial applications, although there is scarce knowledge about these enzymes at the molecular level, including their catalytic and substrate-binding sites. While this lack of knowledge hinders engineering efforts to modify the enzymes, many tannases have been isolated from various fungal strains in a search for the desired enzymatic properties. Here, the first crystal structure of a fungal tannase, that from Aspergillus niger, is reported. The enzyme possesses a typical α/β-hydrolase-fold domain with a large inserted cap domain, which together form a bowl-shaped hemispherical shape with a surface concavity surrounded by N-linked glycans. Gallic acid is bound at the junction of the two domains within the concavity by forming two hydrogen-bonding networks with neighbouring residues. One is formed around the carboxyl group of the gallic acid and involves residues from the hydrolase-fold domain, including those from the catalytic triad, which consists of Ser206, His485 and Asp439. The other is formed around the three hydroxyl groups of the compound, with the involvement of residues mainly from the cap domain, including Gln238, Gln239, His242 and Ser441. Gallic acid is bound in a sandwich-like mode by forming a hydrophobic contact with Ile442. All of these residues are found to be highly conserved among fungal and yeast tannases.
机译：丹宁酸酶是最初的丝氨酸酯酶真菌中发现超过一半几个世纪前。在鞣花鞣质gallolyl酯债券没食子酸释放,这是一个重要的中间在化学和制药行业。丹宁酸酶发现广泛的工业应用,虽然缺乏这些知识酶在分子水平上,包括他们催化和substrate-binding网站。缺乏知识阻碍了工程的努力修改的酶,许多丹宁酸酶从各种真菌分离株在搜索对所需的酶学性质。第一个真菌丹宁酸酶的晶体结构,从黑曲霉,报道。拥有一个典型的α/β-hydrolase-fold域大帽域插入,在一起形成一个碗状半球形表面凹度N-linked聚糖包围。没食子酸结的两个域内形成的凹度两个氢键网络与邻国残留。没食子酸和涉及的残留物hydrolase-fold域,包括催化三分子,包括Ser206 His485和Asp439。羟基的化合物,残留的参与主要的帽子域,包括Gln238 Gln239 His242和Ser441。模式形成疏水接触Ile442。真菌和酵母中高度保守的丹宁酸酶。

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