7MOJ
Crystal Structure of Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1(AtPFA-DSP1 ) Cys150Ser in complex with a metaphosphate intermediate
Summary for 7MOJ
| Entry DOI | 10.2210/pdb7moj/pdb |
| Descriptor | Tyrosine-protein phosphatase DSP1, PHOSPHITE ION (3 entities in total) |
| Functional Keywords | inositol, inositol pyrophosphate, transferase, hydrolase, cell-signaling, phosphatase, substrate recognition, reaction mechanism, intermediate, phosphate, metaphosphate, molecular dynamic simulation, self-activation, catalytic water |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 39443.48 |
| Authors | Wang, H.,Shears, S.B. (deposition date: 2021-05-01, release date: 2022-03-02, Last modification date: 2024-05-22) |
| Primary citation | Wang, H.,Perera, L.,Jork, N.,Zong, G.,Riley, A.M.,Potter, B.V.L.,Jessen, H.J.,Shears, S.B. A structural expose of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop. Nat Commun, 13:2231-2231, 2022 Cited by PubMed Abstract: Structural snapshots of protein/ligand complexes are a prerequisite for gaining atomic level insight into enzymatic reaction mechanisms. An important group of enzymes has been deprived of this analytical privilege: members of the protein tyrosine phosphatase (PTP) superfamily with catalytic WPD-loops lacking the indispensable general-acid/base within a tryptophan-proline-aspartate/glutamate context. Here, we provide the ligand/enzyme crystal complexes for one such PTP outlier: Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1 (AtPFA-DSP1), herein unveiled as a regioselective and efficient phosphatase towards inositol pyrophosphate (PP-InsP) signaling molecules. Although the WPD loop is missing its canonical tripeptide motif, this structural element contributes to catalysis by assisting PP-InsP delivery into the catalytic pocket, for a choreographed exchange with phosphate reaction product. Subsequently, an intramolecular proton donation by PP-InsP substrate is posited to substitute functionally for the absent aspartate/glutamate general-acid. Overall, we expand mechanistic insight into adaptability of the conserved PTP structural elements. PubMed: 35468885DOI: 10.1038/s41467-022-29673-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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