8SLT
Crystal structure of human STEP (PTPN5) at physiological temperature (310 K) and ambient pressure (0.1 MPa)
Summary for 8SLT
| Entry DOI | 10.2210/pdb8slt/pdb |
| Descriptor | Tyrosine-protein phosphatase non-receptor type 5, SULFATE ION (3 entities in total) |
| Functional Keywords | ptpn5, step, phosphatase, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 32710.11 |
| Authors | Ebrahim, A.,Guerrero, L.,Riley, B.T.,Kim, M.,Huang, Q.,Finke, A.D.,Keedy, D.A. (deposition date: 2023-04-24, release date: 2023-06-21, Last modification date: 2023-09-27) |
| Primary citation | Guerrero, L.,Ebrahim, A.,Riley, B.T.,Kim, M.,Huang, Q.,Finke, A.D.,Keedy, D.A. Pushed to extremes: distinct effects of high temperature vs. pressure on the structure of an atypical phosphatase. Biorxiv, 2023 Cited by PubMed Abstract: Protein function hinges on small shifts of three-dimensional structure. Elevating temperature or pressure may provide experimentally accessible insights into such shifts, but the effects of these distinct perturbations on protein structures have not been compared in atomic detail. To quantitatively explore these two axes, we report the first pair of structures at physiological temperature vs. high pressure for the same protein, STEP (PTPN5). We show that these perturbations have distinct and surprising effects on protein volume, patterns of ordered solvent, and local backbone and side-chain conformations. This includes novel interactions between key catalytic loops only at physiological temperature, and a distinct conformational ensemble for another active-site loop only at high pressure. Strikingly, in torsional space, physiological temperature shifts STEP toward previously reported active-like states, while high pressure shifts it toward a previously uncharted region. Together, our work argues that temperature and pressure are complementary, powerful, fundamental macromolecular perturbations. PubMed: 37205580DOI: 10.1101/2023.05.02.538097 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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