2X13

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

2X13 の概要

• エントリーDOI: 10.2210/pdb2x13/pdb
• 関連するPDBエントリー: 2WZB 2WZC 2WZD 2X14 2X15 2XE6 2XE7 2XE8 2Y3I
• 分子名称: PHOSPHOGLYCERATE KINASE 1, MAGNESIUM ION, 3-PHOSPHOGLYCERIC ACID, ... (5 entities in total)
• 機能のキーワード: transition state analogue, hereditary hemolytic anemia, atp-binding, kinase, glycolysis, transferase, disease mutation
• 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: 45178.99

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: 2009-12-21, 公開日: 2010-12-29, 最終更新日: 2024-08-21)

主引用文献

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

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: 39106858
DOI: 10.1016/j.str.2024.07.007

実験手法

X-RAY DIFFRACTION (1.74 Å)