2WZC

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP, 3PG and aluminium tetrafluoride

2WZC の概要

• エントリーDOI: 10.2210/pdb2wzc/pdb
• 関連するPDBエントリー: 2WZB 2WZD
• 分子名称: PHOSPHOGLYCERATE KINASE 1, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: hereditary hemolytic anemia, transferase, phosphoprotein, kinase, glycolysis, nucleotide-binding
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: P00558
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45317.42

構造登録者

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. (登録日: 2009-11-27, 公開日: 2010-04-14, 最終更新日: 2023-12-20)

主引用文献

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

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: 20397725
DOI: 10.1021/JA100974T

実験手法

X-RAY DIFFRACTION (1.5 Å)