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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate
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Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate

机译：Octameric金黄色葡萄球菌的结构与磷酸烯醇丙酮酸烯醇酶在复杂

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摘要

Staphylococcus aureus is a Gram-positive bacterium with strong pathogenicity that causes a wide range of infections and diseases. Enolase is an evolutionarily conserved enzyme that plays a key role in energy production through glycolysis. Additionally, enolase is located on the surface of S. aureus and is involved in processes leading to infection. Here, crystal structures of Sa_enolase with and without bound phosphoenolpyruvate (PEP) are presented at 1.6 and 2.45 angstrom resolution, respectively. The structure reveals an octameric arrangement; however, both dimeric and octameric conformations were observed in solution. Furthermore, enzyme-activity assays show that only the octameric variant is catalytically active. Biochemical and structural studies indicate that the octameric form of Sa_enolase is enzymatically active in vitro and likely also in vivo, while the dimeric form is catalytically inactive and may be involved in other biological processes.
机译：金黄色葡萄球菌是一种革兰氏阳性细菌具有较强的致病性,引起宽感染和疾病的范围。的进化中发挥着关键的酶通过糖酵解作用,能源生产。此外,烯醇酶位于表面金黄色葡萄球菌和主要参与过程感染。Sa_enolase有或没有绑定磷酸烯醇丙酮酸(PEP)为1.6分别和2.45埃分辨率。结构揭示了一个octameric安排;然而,二聚的和octameric构象被观察到的解决方案。酶活性测定表明,只有octameric变体是催化地活跃。生化和结构研究表明,酶学octameric Sa_enolase形式活跃在体外和体内也有可能,二聚的形式是催化地活动可能参与其他生物过程。

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