6E3B
STRUCTURE OF Siw14 CATALYTIC CORE
Summary for 6E3B
| Entry DOI | 10.2210/pdb6e3b/pdb |
| Related | 2q47 |
| Descriptor | Tyrosine-protein phosphatase SIW14, SULFATE ION (3 entities in total) |
| Functional Keywords | dual specificity phosphatase, inositol phosphate, vh1-like phosphatase, hydrolase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 24 |
| Total formula weight | 479017.03 |
| Authors | Florio, T.,Lokareddy, R.,Cingolani, G. (deposition date: 2018-07-13, release date: 2019-02-27, Last modification date: 2023-10-11) |
| Primary citation | Florio, T.J.,Lokareddy, R.K.,Gillilan, R.E.,Cingolani, G. Molecular Architecture of the Inositol Phosphatase Siw14. Biochemistry, 58:534-545, 2019 Cited by PubMed Abstract: Siw14 is a recently discovered inositol phosphatase implicated in suppressing prion propagation in Saccharomyces cerevisiae. In this paper, we used hybrid structural methods to decipher Siw14 molecular architecture. We found the protein exists in solution as an elongated monomer that is ∼140 Å in length, containing an acidic N-terminal domain and a basic C-terminal dual-specificity phosphatase (DSP) domain, structurally similar to the glycogen phosphatase laforin. The two domains are connected by a protease susceptible linker and do not interact in vitro. The crystal structure of Siw14-DSP reveals a highly basic phosphate-binding loop and an ∼10 Å deep substrate-binding crevice that evolved to dephosphorylate pyro-phosphate moieties. A pseudoatomic model of the full-length phosphatase generated from solution, crystallographic, biochemical, and modeling data sheds light on the interesting zwitterionic nature of Siw14, which we hypothesized may play a role in discriminating negatively charged inositol phosphates. PubMed: 30548067DOI: 10.1021/acs.biochem.8b01044 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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