2WZB
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP, 3PG and magnesium trifluoride
Summary for 2WZB
| Entry DOI | 10.2210/pdb2wzb/pdb |
| Related | 2WZC 2WZD |
| Descriptor | PHOSPHOGLYCERATE KINASE 1, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total) |
| Functional Keywords | hereditary hemolytic anemia, transferase, phosphoprotein, kinase, glycolysis, nucleotide-binding |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm: P00558 |
| Total number of polymer chains | 1 |
| Total formula weight | 45295.74 |
| Authors | Bowler, M.W.,Cliff, M.J.,Marston, J.P.M.,Baxter, N.J.,Hownslow, A.M.H.,Varga, A.V.,Szabo, J.,Vas, M.,Blackburn, G.M.,Waltho, J.P. (deposition date: 2009-11-27, release date: 2010-04-14, Last modification date: 2023-12-20) |
| Primary citation | Cliff, M.J.,Bowler, M.W.,Szabo, J.,Marston, J.P.M.,Varga, A.V.,Hownslow, A.M.H.,Baxter, N.J.,Blackburn, G.M.,Vas, M.,Waltho, J.P. Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis. J.Am.Chem.Soc., 132:6507-, 2010 Cited by PubMed Abstract: Transition state analogue (TSA) complexes formed by phosphoglycerate kinase (PGK) have been used to test the hypothesis that balancing of charge within the transition state dominates enzyme-catalyzed phosphoryl transfer. High-resolution structures of trifluoromagnesate (MgF(3)(-)) and tetrafluoroaluminate (AlF(4)(-)) complexes of PGK have been determined using X-ray crystallography and (19)F-based NMR methods, revealing the nature of the catalytically relevant state of this archetypal metabolic kinase. Importantly, the side chain of K219, which coordinates the alpha-phosphate group in previous ground state structures, is sequestered into coordinating the metal fluoride, thereby creating a charge environment complementary to the transferring phosphoryl group. In line with the dominance of charge balance in transition state organization, the substitution K219A induces a corresponding reduction in charge in the bound aluminum fluoride species, which changes to a trifluoroaluminate (AlF(3)(0)) complex. The AlF(3)(0) moiety retains the octahedral geometry observed within AlF(4)(-) TSA complexes, which endorses the proposal that some of the widely reported trigonal AlF(3)(0) complexes of phosphoryl transfer enzymes may have been misassigned and in reality contain MgF(3)(-). PubMed: 20397725DOI: 10.1021/JA100974T PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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