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

ABSTRACT: The PgdS enzyme is a poly-?-glutamic (?-PGA) hydrolase, which has potential application for a controllable degradation of ?-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 ?-PGA degradation by the PgdS hydrolase and may provide valuable practical information.

SUBMITTER: Zeng J

PROVIDER: S-EPMC5880399 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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

Zeng Jumei J Jin Yun Y Liu Zhongchuan Z

PloS one 20180402 4

The PgdS enzyme is a poly-γ-glutamic (γ-PGA) hydrolase, which has potential application for a controllable degradation of γ-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 m ...[more]

PMID: 29608608

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