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首页> 外文期刊>Journal of Molecular Biology >Novel Mechanism for Cyclic Dinucleotide Degradation Revealed by Structural Studies of Vibrio Phosphodiesterase V-cGAP3
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Novel Mechanism for Cyclic Dinucleotide Degradation Revealed by Structural Studies of Vibrio Phosphodiesterase V-cGAP3

机译：乙二虫磷酸二酯酶V-CGAP3结构研究揭示了循环二核苷酸降解的新机制

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摘要

3'3'-cyclic GMP-AMP (3'3'-cGAMP) belongs to a family of the bacterial secondary messenger cyclic dinucleotides. It was first discovered in the Vibrio cholerae seventh pandemic strains and is involved in efficient intestinal colonization and chemotaxis regulation. Phosphodiesterases (PDEs) that degrade 3'3'-cGAMP play important regulatory roles in the relevant signaling pathways, and a previous study has identified three PDEs in V. cholerae, namely, V-cGAP1, V-cGAP2, and V-cGAP3, functioning in 3'3'-cGAMP degradation. We report the crystal structure, biochemical, and structural analyses of V-cGAP3, providing a foundation for understanding the mechanism of 3'3'-cGAMP degradation and regulation in general. Our crystal and molecular dynamic (MD)-simulated structures revealed that V-cGAP3 contains tandem HD-GYP domains within its N-and C-terminal domains, with similar three-dimensional topologies despite their low-sequence identity. Biochemical and structural analyses showed that the N-terminal domain plays a mechanism of positive regulation for the catalytic C-terminal domain. We also demonstrated that the other homologous Vibrio PDEs, V-cGAP1/2, likely function via a similar mechanism. (C) 2018 Published by Elsevier Ltd.
机译：3'3'-Cyclic GMP-AMP（3'3'-CGAMP）属于细菌次要信使循环二核苷酸的家族。首先在霍乱霍乱七大流行菌株中发现，参与有效的肠道殖民化和趋化性调节。磷酸二酯酶（PDE）降解3'3'-cgamp在相关的信号通路中起重要的调节作用，并且先前的研究已经确定了V.霍乱，即V-CGAP1，V-CGAP2和V-CGAP3中的三个PDE。在3'3'-cgamp降解中的功能。我们报告了V-CGAP3的晶体结构，生化和结构分析，为了解3'3'-CGAMP降解和调节的机制，提供了基础。我们的晶体和分子动态（MD）刺激的结构显示V-CGAP3含有其N-和C末端域内的串联HD-GYMa8，尽管它们的低序列标识，但仍具有相似的三维拓扑。生物化学和结构分析表明，N-末端结构域对催化C末端结构域的正调节作用。我们还证明，其他同源振动PDE，V-CGAP1 / 2，可能通过类似机制功能。 （c）2018年由elestvier有限公司发布

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