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第三类杂交集群蛋白质的同位体结构显示了与Ni,Fe-一氧化碳脱基酶的进化关系
Takashi Fujishiro1, Kyosei Takaoka2
1Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Shimo-Okubo 255, Sakura-ku, Saitama, 338-8570, Japan. tfujishiro@mail.saitama-u.ac.jp.
Nature communications
|September 14, 2023
概括
这项研究揭示了来自Metanothermobacter marburgensis的III类混合群蛋白 (HCP) 的结构,显示其与一氧化碳脱酶 (CODHs) 的相似性. 这项研究强调了Cys67在HCP功能和金属集群结合中的关键作用.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 生物有机化学 生物有机化学
背景情况:
- 混合集群蛋白 (HCP) 是含有独特Fe-S-O集群的金属酶.
- 有三种类别的HCPs,其中III类是同位体的,并且与Ni,Fe-碳一氧化物脱酶 (CODHs) 结构相关.
研究的目的:
- 为了确定来自Mm HCP的Methanothermobacter marburgensis (Mm HCP) 的III类HCP的X射线晶体结构.
- 为了比较Mm HCP与CODH和其他HCP类别的结构.
- 调查Cys67在MM HCP结构和活动中的作用.
主要方法:
- 进行X射线晶体学以确定Mm HCP的3D结构.
- 在MM HCP,CODH和其他HCP类别之间进行结构比较.
- 包括Cys67突变在内的Mm HCP变体的生物化学表征.
- 基于结构的生物信息学分析.
主要成果:
- 第三类MM HCP的晶体结构显示了类似于CODHs的同位体结构.
- [4Fe-4S]和混合集群在不同的HCP类中占据了同等位置.
- 在MM HCP和CODHs的同位体接口和活性部位上发现了独特的特征.
- 发现Cys67对Mm HCP结构,金属集群结合和xylamine减少酶活性至关重要.
结论:
- 该研究阐明了III类HCP职能的结构基础及其与CODHs的关系.
- 这些发现为HCP/CODH超级家族的结构演变提供了洞察力.
- Cys67对于Mm HCP的催化活性至关重要.
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