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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >The crystal structure of AjiA1 reveals a novel structural motion mechanism in the adenylate-forming enzyme family
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The crystal structure of AjiA1 reveals a novel structural motion mechanism in the adenylate-forming enzyme family

机译：AjiA1揭示小说的晶体结构结构的运动机制adenylate-forming酶家族

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摘要

Adenylate-forming enzymes (AFEs) are a mechanistic superfamily of proteins that are involved in many cellular roles. In the biosynthesis of benzoxazole antibiotics, an AFE has been reported to play a key role in the condensation of cyclic molecules. In the biosynthetic gene cluster for the benzoxazole AJI9561, AjiA1 catalyzes the condensation of two 3-hydroxyanthranilic acid (3-HAA) molecules using ATP as a co-substrate. Here, the enzymatic activity of AjiA1 is reported together with a structural analysis of its apo form. The structure of AjiA1 was solved at 2.0 A resolution and shows a conserved fold with other AFE family members. AjiA1 exhibits activity in the presence of 3-HAA (Km = 77.86 ± 28.36, kcat = 0.04 ± 0.004) and also with the alternative substrate 3-hydroxybenzoic acid (3-HBA; Km = 22.12 ± 31.35, kcat = 0.08 ± 0.005). The structure of AjiA1 in the apo form also reveals crucial conformational changes that occur during the catalytic cycle of this enzyme which have not been described for any other AFE member. Consequently, the results shown here provide insights into this protein family and a new subgroup is proposed for enzymes that are involved in benzoxazole-ring formation.
机译：Adenylate-forming酶(af)是机械的总科的蛋白质参与了许多细胞的作用。苯并恶唑抗生素,AFE报道扮演一个关键的角色在循环的冷凝分子。苯并恶唑的AJI9561, AjiA1催化两个3-hydroxyanthranilic酸的缩合使用ATP作为co-substrate (3-HAA)分子。在这里,AjiA1报道的酶活性在一起的结构分析的形式。分辨率和显示了守恒的褶皱与其他安全的家庭成员。的存在3-HAA(公里= 77.86±28.36,kcat =0.04±0.004)也与选择衬底3-hydroxybenzoic酸(3-HBA;22.12±31.35,kcat = 0.08±0.005)。结构的AjiA1 apo形式也揭示了关键过程发生构象变化的影响没有这种酶的催化循环被描述的任何其他安全的成员。因此,这里提供的结果洞察这种蛋白质的家人和一个新的小组提出了酶参与benzoxazole-ring形成。

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