在其SAR域的膜释放后,二硫化物异构化激活了P1溶酶
Min Xu1, Arockiasamy Arulandu, Douglas K Struck
1Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.
概括
大肠杆菌中的P1溶酶 (Lyz) 在细胞膜中保持不活跃,直到被P1holin释放. 在释放后,Lyz经历了结构变化和二硫化物键重组以激活.
科学领域:
- 细菌生物学的生物学
- 分子微生物学分子微生物学
- 蛋白质的结构和功能.
背景情况:
- P1溶酶 (Lyz) 是一种内溶酶,分泌到大肠杆菌的周围质中.
- 在菌体P1复制之前,lys 积聚在一个不活跃的,与膜结合的形式.
- 这种不活性状态对于控制溶解和菌体释放至关重要.
研究的目的:
- 阐明控制P1溶酶 (Lyz) 激活的机制.
- 研究与Lyz激活相关的结构和生化变化.
- 了解信号停止释放 (SAR) 域在lys调节中的作用.
主要方法:
- 对P1 Lyz.的遗传和生化分析.
- 确定非活性和活性Lyz形式的晶体结构.
- 在SAR域中对硫化-二硫化物异构的表征.
主要成果:
- 通过拓学,构造学和共价性控制,P1 Lyz 保持在非活性状态.
- 通过P1holin从膜中释放会触发Lyz激活.
- 激活涉及依赖于N端SAR域cysteine的分子内硫酸二醇异构.
结论:
- P1 Lyz激活是一个多步骤的过程,由膜结合和P1 holin.调节.
- 在Lyz中,结构和二硫化物键的重新排列对于其催化活性至关重要.
- SAR域在调节P1内分泌酶的激活中起着至关重要的作用.
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