Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.
Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.
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DOI：
10.1107/s2053230x23006672
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发表时间：
2023-09-01
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来自皮炎放线菌的亚胺还原酶的结构以三种晶体形式呈现，每种晶体形式都提供有关酶内构象动力学以及辅因子和底物结合的信息。来自皮炎拟酵母 (AdRedAm) 的 NADPH 依赖性亚胺还原酶可催化某些酮与等摩尔比的胺供体进行还原胺化。 AdRedAm 的结构已确定为三种形式。第一种形式属于 P3121 空间群，并被精化至 2.01 Å 分辨率，在不对称单元中具有两个分子（一个二聚体），与氧化还原非活性辅因子 NADPH4 形成复合物。第二种形式属于 C21 空间群，分辨率精化至 1.73 Å，不对称单元中有九个分子（四个半二聚体），每个分子都与 NADP+ 复合。第三种形式属于 P3121 空间群，分辨率精化至 1.52 Å，不对称单元中有一个分子（一个半二聚体）。该结构再次与 NADP+ 以及底物 2,2-二氟苯乙酮复合。不同的数据集允许分析不同构象状态的 AdRedAm，并且还揭示了酶转化氟化苯乙酮底物时立体选择性的分子基础。
The structure of the imine reductase from A. dermatitidis is presented in three crystal forms, each of which provides information on conformational dynamics and cofactor and substrate binding within the enzyme. The NADPH-dependent imine reductase from Ajellomyces dermatitidis (AdRedAm) catalyzes the reductive amination of certain ketones with amine donors supplied in an equimolar ratio. The structure of AdRedAm has been determined in three forms. The first form, which belongs to space group P3121 and was refined to 2.01 Å resolution, features two molecules (one dimer) in the asymmetric unit in complex with the redox-inactive cofactor NADPH4. The second form, which belongs to space group C21 and was refined to 1.73 Å resolution, has nine molecules (four and a half dimers) in the asymmetric unit, each complexed with NADP+. The third form, which belongs to space group P3121 and was refined to 1.52 Å resolution, has one molecule (one half-dimer) in the asymmetric unit. This structure was again complexed with NADP+ and also with the substrate 2,2-difluoroacetophenone. The different data sets permit the analysis of AdRedAm in different conformational states and also reveal the molecular basis of stereoselectivity in the transformation of fluorinated acetophenone substrates by the enzyme.