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

被引：3
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
收藏
页数：13
相关论文
共 40 条
[1]   Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes [J].
Anantharaman, V ;
Aravind, L .
GENOME BIOLOGY, 2003, 4 (02)
[2]   Solution Structure of IseA, an Inhibitor Protein of DL-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop [J].
Arai, Ryoichi ;
Fukui, Sadaharu ;
Kobayashi, Naoya ;
Sekiguchi, Junichi .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (53) :44736-44748
[3]   Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli:: Structural evidence for a novel cysteine peptidase catalytic triad [J].
Aramini, James M. ;
Rossi, Paolo ;
Huang, Yuanpeng J. ;
Zhao, Li ;
Jiang, Mei ;
Maglaqui, Melissa ;
Xiao, Rong ;
Locke, Jessica ;
Nair, Rajesh ;
Rost, Burkhard ;
Acton, Thomas B. ;
Inouye, Masayori ;
Montelione, Gaetano T. .
BIOCHEMISTRY, 2008, 47 (37) :9715-9717
[4]   Poly (glutamic acid) - An emerging biopolymer of commercial interest [J].
Bajaj, Ishwar ;
Singhal, Rekha .
BIORESOURCE TECHNOLOGY, 2011, 102 (10) :5551-5561
[5]   Bacillus subtilis natto: a non-toxic source of poly-γ-glutamic acid that could be used as a cryoprotectant for probiotic bacteria [J].
Bhat, Aditya R. ;
Irorere, Victor U. ;
Bartlett, Terry ;
Hill, David ;
Kedia, Gopal ;
Morris, Mark R. ;
Charalampopoulos, Dimitris ;
Radecka, Iza .
AMB EXPRESS, 2013, 3 :1-9
[6]   SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information [J].
Biasini, Marco ;
Bienert, Stefan ;
Waterhouse, Andrew ;
Arnold, Konstantin ;
Studer, Gabriel ;
Schmidt, Tobias ;
Kiefer, Florian ;
Cassarino, Tiziano Gallo ;
Bertoni, Martino ;
Bordoli, Lorenza ;
Schwede, Torsten .
NUCLEIC ACIDS RESEARCH, 2014, 42 (W1) :W252-W258
[7]   ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments [J].
Bond, Charles Simon ;
Schuettelkopf, Alexander Wolfgang .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2009, 65 :510-512
[8]   Scalable web services for the PSIPRED Protein Analysis Workbench [J].
Buchan, Daniel W. A. ;
Minneci, Federico ;
Nugent, Tim C. O. ;
Bryson, Kevin ;
Jones, David T. .
NUCLEIC ACIDS RESEARCH, 2013, 41 (W1) :W349-W357
[9]   Glutamic acid independent production of poly-γ-glutamic acid by Bacillus amyloliquefaciens LL3 and cloning of pgsBCA genes [J].
Cao, Mingfeng ;
Geng, Weitao ;
Liu, Li ;
Song, Cunjiang ;
Xie, Hui ;
GuoA, Wenbin ;
Jin, Yinghong ;
Wang, Shufang .
BIORESOURCE TECHNOLOGY, 2011, 102 (05) :4251-4257
[10]   MUSCLE: multiple sequence alignment with high accuracy and high throughput [J].
Edgar, RC .
NUCLEIC ACIDS RESEARCH, 2004, 32 (05) :1792-1797
1234