Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments,Acta Crystallographica Section F

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Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments
Acta Crystallographica Section F ( IF 1.1 ) Pub Date : 2021-09-02 , DOI: 10.1107/s2053230x21007470
Jessica M Ochoa ₁ , Oscar Mijares ₂ , Andrea A Acosta ₂ , Xavier Escoto ₃ , Nancy Leon-Rivera ₂ , Joanna D Marshall ₃ , Michael R Sawaya ₄ , Todd O Yeates ₁

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Bacterial microcompartments are large supramolecular structures comprising an outer proteinaceous shell that encapsulates various enzymes in order to optimize metabolic processes. The outer shells of bacterial microcompartments are made of several thousand protein subunits, generally forming hexameric building blocks based on the canonical bacterial microcompartment (BMC) domain. Among the diverse metabolic types of bacterial microcompartments, the structures of those that use glycyl radical enzymes to metabolize choline have not been adequately characterized. Here, six structures of hexameric shell proteins from type I and type II choline-utilization microcompartments are reported. Sequence and structure analysis reveals electrostatic surface properties that are shared between the four types of shell proteins described here.

中文翻译：

两种胆碱利用细菌微区室六聚壳蛋白的结构表征

细菌微区室是大型超分子结构，包含蛋白质外壳，其中封装了各种酶以优化代谢过程。细菌微区室的外壳由数千个蛋白质亚基组成，通常形成基于典型细菌微区室（BMC）结构域的六聚体构建块。在细菌微区室的多种代谢类型中，利用甘氨酰自由基酶代谢胆碱的细菌微区室的结构尚未得到充分表征。在此，报道了来自 I 型和 II 型胆碱利用微区室的六聚壳蛋白的六种结构。序列和结构分析揭示了此处描述的四种类型的壳蛋白共有的静电表面特性。

更新日期：2021-09-02

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