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在TEM-1和CTX-M-9β-乳酸酶中二硫化键形成的不同影响

Miranda Villanueva¹, Lauren E Vostal¹, Drew N Cohen¹

¹Department of Chemistry, Williams College, Williamstown, Massachusetts, USA.

Protein science : a publication of the Protein Society

|October 28, 2023

概括

在β-乳糖酶中的工程二硫化键改变了它们的蛋白质能量格局. 引入二硫化键意外诱导CTX-M-9的寡合化,而不是稳定,突出了蛋白质稳定策略的局限性.

科学领域:

生物化学生物化学
蛋白质工程是指蛋白质工程.
结构生物学结构生物学

背景情况:

二硫化键影响蛋白质的结构和稳定性.
β-乳酸酶酶TEM-1和CTX-M-9表现出不同的热力学稳定性和平衡状态.
在TEM-1中存在固有的二硫化物键,而在CTX-M-9中则没有.

研究的目的:

研究二硫化物键对蛋白质能量景观的影响.
确定二硫化物键是否是TEM-1和CTX-M-9β-lactamases之间不同能量场景的主要原因.

主要方法:

突变酶被用来从TEM-1中去除二硫化物键,并将其引入CTX-M-9.
在不同条件下 (例如尿素) 分析了平衡状态人群.
通过比较氧化单体与无氨酸变体来评估蛋白质稳定性.

主要成果:

修改二硫化物键改变了TEM-1中平衡状态的稳定性和群体.
在CTX-M-9中,通过引入二硫化物键,诱导了一种新的,活跃的,高阶的寡合体状态.
引入的二硫化物键并没有稳定CTX-M-9,与TEM-1中的原生键不同.

结论:

双硫化物键工程在蛋白质稳定方面并不普遍有效.
微小的序列修改可以导致复杂的homo-oligomerization.
蛋白质复合体的形成可能是一个常见的进化途径.

关键词:

一个A类β-乳酸酶.硫化二氧化物工程是什么意思折叠中间产品的折叠中间产品的折叠蛋白质设计蛋白质设计蛋白质的热力学稳定性热力学稳定性

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