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通过进化合分析解析的糖聚合酶RodA的结构

Megan Sjodt¹, Kelly Brock², Genevieve Dobihal³

¹Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

|March 29, 2018

概括

研究人员确定了RodA蛋白的晶体结构,RodA蛋白是细菌细胞壁合成中的关键酶. 这种结构揭示了Roda必不可少的关键腔.

科学领域:

结构生物学
微生物学
生物化学

背景情况:

形状,延长,分裂和分泌 (SEDS) 蛋白质是细菌细胞壁生物学中涉及的必不可少的跨膜酶.
最近的研究确定了Roda,一个原型的SEDS蛋白质,作为糖酶,挑战了以前对青素结合蛋白的归因.
包括Roda在内的SEDS蛋白正在成为新型抗生素的潜在点,但它们的分子机制在很大程度上仍未被阐明.

研究的目的:

为了确定Thermus thermophilus RodA蛋白的高分辨率晶体结构.
研究SEDS蛋白功能的分子基础,并确定具有催化作用的重要区域.
为了解细菌细胞壁合成和开发新的治疗策略提供结构框架.

主要方法:

在2.9 Å分辨率下确定Thermus thermophilus RodA的晶体结构,使用基于进化共变的折叠预测来进行分子替代.
通过膜折叠,细胞外环和Roda结构中的保存腔的分析.
在Bacillus subtilis和Escherichia coli体内进行体外和体内突变的实验,以评估发现的腔的功能重要性.

主要成果:

晶体结构显示出具有显著的细胞外循环结构的十通透膜折叠.
在跨膜域内发现了一个高度保守的腔体,其结构类似于跨膜受体中的配体结合位.
在体外酶测定和体内细胞研究中,通过突变发生的这种保存腔的扰乱取消了Roda功能.

结论:

确定Roda的结构为SEDS蛋白家族提供了前所未有的分子洞察力.
已识别的跨膜腔对于Roda的糖聚合酶活性和细菌细胞壁合成至关重要.
这些发现为了解细菌细胞包膜生物发生提供了结构基础,并指导针对SEDS蛋白的新型抗生素的开发.

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