5O7F
Structure of the inactive T.maritima PDE (TM1595) D80N D154N mutant with GMP and Mn2+
Summary for 5O7F
| Entry DOI | 10.2210/pdb5o7f/pdb |
| Related | 5O1U 5O25 5O4Z 5O58 5O70 |
| Descriptor | phosphodiesterase, GUANOSINE-5'-MONOPHOSPHATE, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | phosphodiesterase, hydrolase |
| Biological source | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
| Total number of polymer chains | 2 |
| Total formula weight | 77056.49 |
| Authors | Witte, G.,Drexler, D.,Mueller, M. (deposition date: 2017-06-08, release date: 2017-10-25, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 29107484DOI: 10.1016/j.str.2017.10.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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