5O4Z

Structure of the inactive T.maritima PDE (TM1595) D80N D154N mutant with substrate 5'-pApA

5O4Z の概要

• エントリーDOI: 10.2210/pdb5o4z/pdb
• 関連するPDBエントリー: 5O1U 5O25
• 分子名称: DHH/DHHA1-type phosphodiesterase TM1595, ADENOSINE-5'-MONOPHOSPHATE, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: phosphodiesterase, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39394.86

構造登録者

Witte, G.,Drexler, D.,Mueller, M. (登録日: 2017-05-31, 公開日: 2017-10-25, 最終更新日: 2024-01-17)

主引用文献

Drexler, D.J.,Muller, M.,Rojas-Cordova, C.A.,Bandera, A.M.,Witte, G.
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima.
Structure, 25:1887-1897.e4, 2017

PubMed Abstract: The concentration of messenger molecules in bacterial cells needs to be tightly regulated. This can be achieved by either controlling the synthesis rate, degradation, or export by specific transporters, respectively. The regulation of the essential second messenger c-di-AMP is achieved by modulation of the diadenylate cyclase activity as well as by specific phosphodiesterases that hydrolyze c-di-AMP in the cell. We provide here structural and biochemical data on the DHH-type phosphodiesterase TmPDE (TM1595) from Thermotoga maritima. Our analysis shows that TmPDE is preferentially degrading linear dinucleotides, such as 5'-pApA, 5'-pGpG, and 5'-pApG, compared with cyclic dinucleotide substrates. The high-resolution structural data provided here describe all steps of the PDE reaction: the ligand-free enzyme, two substrate-bound states, and three post-reaction states. We can furthermore show that Pde2 from Streptococcus pneumoniae shares both structural features and substrate specificity based on small-angle X-ray scattering data and biochemical assays.

PubMed: 29107484
DOI: 10.1016/j.str.2017.10.001

実験手法

X-RAY DIFFRACTION (1.7 Å)