3ZI4
The structure of Beta-phosphoglucomutase Inhibited With Glucose-6-phosphate and Scandium Tetrafluoride
Summary for 3ZI4
| Entry DOI | 10.2210/pdb3zi4/pdb |
| Descriptor | BETA-PHOSPHOGLUCOMUTASE, MAGNESIUM ION, 6-O-phosphono-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | isomerase, scandium tetrafluoride, experimental phasing, phosphoryl transfer |
| Biological source | LACTOCOCCUS LACTIS |
| Cellular location | Cytoplasm : P71447 |
| Total number of polymer chains | 1 |
| Total formula weight | 24644.99 |
| Authors | Pellegrini, E.,Bowler, M.W. (deposition date: 2013-01-03, release date: 2014-01-15, Last modification date: 2024-08-21) |
| Primary citation | Pellegrini, E.,Juyoux, P.,von Velsen, J.,Baxter, N.J.,Dannatt, H.R.W.,Jin, Y.,Cliff, M.J.,Waltho, J.P.,Bowler, M.W. Metal fluorides-multi-functional tools for the study of phosphoryl transfer enzymes, a practical guide. Structure, 2024 Cited by PubMed Abstract: Enzymes facilitating the transfer of phosphate groups constitute the most extensive protein families across all kingdoms of life. They make up approximately 10% of the proteins found in the human genome. Understanding the mechanisms by which enzymes catalyze these reactions is essential in characterizing the processes they regulate. Metal fluorides can be used as multifunctional tools to study these enzymes. These ionic species bear the same charge as phosphate and the transferring phosphoryl group and, in addition, allow the enzyme to be trapped in catalytically important states with spectroscopically sensitive atoms interacting directly with active site residues. The ionic nature of these phosphate surrogates also allows their removal and replacement with other analogs. Here, we describe the best practices to obtain these complexes, their use in NMR, X-ray crystallography, cryo-EM, and SAXS and describe a new metal fluoride, scandium tetrafluoride, which has significant anomalous signal using soft X-rays. PubMed: 39106858DOI: 10.1016/j.str.2024.07.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.33 Å) |
Structure validation
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