7L36
PEPCK steady-state structure with Mn and GTP
Summary for 7L36
| Entry DOI | 10.2210/pdb7l36/pdb |
| Descriptor | Phosphoenolpyruvate carboxykinase, cytosolic [GTP], MANGANESE (II) ION, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | pepck, phosphoenolpyruvate carboxykinase, gluconeogensis, lyase |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 70367.24 |
| Authors | Clinger, J.A.,Moreau, D.W.,McLeod, M.J.,Holyoak, T.,Thorne, R.E. (deposition date: 2020-12-17, release date: 2021-10-13, Last modification date: 2023-10-18) |
| Primary citation | Clinger, J.A.,Moreau, D.W.,McLeod, M.J.,Holyoak, T.,Thorne, R.E. Millisecond mix-and-quench crystallography (MMQX) enables time-resolved studies of PEPCK with remote data collection. Iucrj, 8:784-792, 2021 Cited by PubMed Abstract: Time-resolved crystallography of biomolecules in action has advanced rapidly as methods for serial crystallography have improved, but the large number of crystals and the complex experimental infrastructure that are required remain serious obstacles to its widespread application. Here, millisecond mix-and-quench crystallography (MMQX) has been developed, which yields millisecond time-resolved data using far fewer crystals and routine remote synchrotron data collection. To demonstrate the capabilities of MMQX, the conversion of oxaloacetic acid to phosphoenolpyruvate by phosphoenolpyruvate carboxy-kinase (PEPCK) is observed with a time resolution of 40 ms. By lowering the entry barrier to time-resolved crystallography, MMQX should enable a broad expansion in structural studies of protein dynamics. PubMed: 34584739DOI: 10.1107/S2052252521007053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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