Crystal structures of γ-glutamylmethylamide synthetase provide insight into bacterial metabolism of oceanic monomethylamine
العنوان: | Crystal structures of γ-glutamylmethylamide synthetase provide insight into bacterial metabolism of oceanic monomethylamine |
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المؤلفون: | Yin Chen, Qing-Tao Shen, Peng Wang, Na Zhang, Ning Wang, Gui-Peng Yang, Shengying Li, Chun-Yang Li, Ming Peng, Xiu-Lan Chen, Yu-Zhong Zhang, Fuchuan Li, Chao Gao |
المصدر: | The Journal of Biological Chemistry |
بيانات النشر: | Elsevier BV, 2021. |
سنة النشر: | 2021 |
مصطلحات موضوعية: | 0301 basic medicine, Conformational change, Microbial metabolism, Protein Data Bank (RCSB PDB), Biochemistry, GS, glutamine synthetase, MetSox, methionine sulfoximine, Adenosine Triphosphate, Deprotonation, Glutamates, MRC, marine Roseobacter clade, Tetrahedral carbonyl addition compound, AMPPNP, phosphoaminophosphonic acid-adenylate ester, QD, Carbon-Nitrogen Ligases, Magnesium, PDB, protein data bank, GMA, γ-glutamylmethylamide, Chemistry, monomethylamine (MMA) metabolism, food and beverages, Editors' Pick, NMG, N-methylglutamate, MetSox-P, methionine sulfoximine phosphate, Research Article, crystal structure, Stereochemistry, Glutamic Acid, Rhodovulum, enzyme catalysis, Catalysis, Enzyme catalysis, Methylamines, 03 medical and health sciences, GmaS, γ-glutamylmethylamide synthetase, Glutamine synthetase, Escherichia coli, enzyme mechanism, Molecular Biology, AMPPCP, phosphomethylphosphonic acid-adenylate ester, RhGmaS, GmaS from Rhodovulum sp. 12E13, 030102 biochemistry & molecular biology, protein complex, bacterial metabolism, Cell Biology, Metabolism, QP, QR, MMA, monomethylamine, Microscopy, Electron, 030104 developmental biology, γ-glutamylmethylamide synthetase (GmaS) |
الوصف: | Monomethylamine (MMA) is an important climate-active oceanic trace gas and ubiquitous in the oceans. γ-Glutamylmethylamide synthetase (GmaS) catalyzes the conversion of MMA to γ-glutamylmethylamide, the first step in MMA metabolism in many marine bacteria. The gmaS gene occurs in ∼23% of microbial genomes in the surface ocean and is a validated biomarker to detect MMA-utilizing bacteria. However, the catalytic mechanism of GmaS has not been studied because of the lack of structural information. Here, the GmaS from Rhodovulum sp. 12E13 (RhGmaS) was characterized, and the crystal structures of apo-RhGmaS and RhGmaS with different ligands in five states were solved. Based on structural and biochemical analyses, the catalytic mechanism of RhGmaS was explained. ATP is first bound in RhGmaS, leading to a conformational change of a flexible loop (Lys287-Ile305), which is essential for the subsequent binding of glutamate. During the catalysis of RhGmaS, the residue Arg312 participates in polarizing the γ-phosphate of ATP and in stabilizing the γ-glutamyl phosphate intermediate; Asp177 is responsible for the deprotonation of MMA, assisting the attack of MMA on γ-glutamyl phosphate to produce a tetrahedral intermediate; and Glu186 acts as a catalytic base to abstract a proton from the tetrahedral intermediate to finally generate glutamylmethylamide. Sequence analysis suggested that the catalytic mechanism of RhGmaS proposed in this study has universal significance in bacteria containing GmaS. Our results provide novel insights into MMA metabolism, contributing to a better understanding of MMA catabolism in global carbon and nitrogen cycles. |
وصف الملف: | application/pdf |
تدمد: | 0021-9258 |
DOI: | 10.1074/jbc.ra120.015952 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65f1d1d3e5f8f69e5d03aa884830e9bd https://doi.org/10.1074/jbc.ra120.015952 |
Rights: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....65f1d1d3e5f8f69e5d03aa884830e9bd |
قاعدة البيانات: | OpenAIRE |
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