Solution scattering study of the Bacillus subtilis PgdS enzyme involved in poly-γ-glutamic acids degradation

被引:2
|
作者
Zeng, Jumei [1 ]
Jin, Yun [1 ]
Liu, Zhongchuan [1 ]
机构
[1] Chinese Acad Sci, Chengdu Inst Biol, Key Lab Environm & Appl Microbiol, Chengdu, Sichuan, Peoples R China
来源
PLOS ONE | 2018年 / 13卷 / 04期
基金
中国国家自然科学基金;
关键词
SMALL-ANGLE SCATTERING; SEQUENCE ALIGNMENT; POLYGLUTAMIC ACID; PROTEIN; RECOGNITION; PRODUCT; GENE; LYTF;
D O I
10.1371/journal.pone.0195355
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The PgdS enzyme is a poly-gamma-glutamic (gamma-PGA) hydrolase, which has potential application for a controllable degradation of gamma-PGA by enzymatic depolymerization; however, the structure of PgdS is still unknown. Here, to study in detail the full-length PgdS structure, we analyze the low-resolution architecture of PgdS hydrolase from Bacillus subtilis in solution using small angle X-ray scattering (SAXS) method. Combining with other methods, like dynamic light scattering and mutagenesis analyses, a model for the full length structure and the possible substrate delivery route of PgdS are proposed. The results will provide useful hints for future investigations into the mechanisms of gamma-PGA degradation by the PgdS hydrolase and may provide valuable practical information.
引用
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页数:13
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