中央β-表中的芳香残留物变化影响大肠杆菌的稳定性和活性 3 葡萄糖素3
Mohammed Shazaly A Elhassan1, Trang Van Tran1,2, ChangWoo Lee1
1Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan 38453, South Korea.
ACS omega
|June 30, 2025
概括
细菌谷氨素Grx3 (EcGrx3) 的芳香残留变化影响蛋白质的稳定性和活性. Phe56对于最佳平衡至关重要,而Tyr6则稳定关键接口,影响结构适应.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 酶学 是一种酶学.
背景情况:
- 细菌谷氨素Grx3 (EcGrx3) 是一种具有柔性氨素 (Trx) 折叠的I类氧化还原酶.
- EcGrx3的稳定性受到Tyr6,Phe56和Arg46.6参与的网络的影响.
研究的目的:
- 研究Tyr6和Phe56中的芳香残留替代物对EcGrx3稳定性和活性的影响.
- 确定在EcGrx3结构-功能关系中阴离子-π相互作用和疏水性包装的作用.
主要方法:
- 局部定向的突变发生产生Phe56和Tyr6变体.
- 热变性和化瓜尼迪尼 (GdmCl) 展开测试,以评估蛋白质的稳定性.
- 酶活性测定和形状灵活性测量.
主要成果:
- 突变降低了化温度,增加了GdmCl的灵敏度,表明稳定性下降.
- 56的替代物对稳定性和活性产生了不同的影响;F56Y显示了与野生类型相似的特性,而F56W提高了催化效率,但降低了稳定性.
- Tyr6F突变显著降低了α-螺旋的含量和催化效率.
结论:
- 芳香残留物Tyr6和Phe56对于EcGrx3的稳定性和α螺旋形成至关重要.
- 通过子-π和疏水相互作用,Phe56提供了稳定性和功能的最佳平衡.
- 在β-叶内的芳香变化驱动Trx-fold超级家族的结构和功能适应.
更多相关视频
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
8.8K
11:04Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
7.4K
相关概念视频
Protein Modifications in the RER
5.6K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.6K
Stringent Response in E. coli
61
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
61
Protein Folding Quality Check in the RER
3.9K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.9K
Diversity of Archaea III
81
Crenarchaeota, a prominent phylum of Archaea, is remarkable for its ability to thrive in extreme environments characterized by high temperatures and acidity. These microorganisms inhabit sulfuric hot springs, volcanic systems, and submarine hydrothermal vents, where temperatures often exceed 100°C. The unique adaptations of Crenarchaeota not only allow survival under such extreme conditions but also provide insights into the mechanisms of life in primordial Earth-like...
81
Ligand Binding and Linkage
4.9K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.9K
Protein Folding
121.7K
Overview
121.7K
