3HQP

Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with ATP, Oxalate and fructose 2,6 bisphosphate

3HQP の概要

• エントリーDOI: 10.2210/pdb3hqp/pdb
• 関連するPDBエントリー: 1PKL 3E0V 3E0W 3HQN 3HQO 3HQQ
• 分子名称: Pyruvate kinase, MAGNESIUM ION, POTASSIUM ION, ... (8 entities in total)
• 機能のキーワード: tim barrel, t-state enzyme, allosteric enzyme, glycolysis, kinase, magnesium, metal-binding, pyruvate, transferase
• 由来する生物種: Leishmania mexicana
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 888389.65

構造登録者

Morgan, H.P.,Walkinshaw, M.D. (登録日: 2009-06-08, 公開日: 2010-02-16, 最終更新日: 2023-11-01)

主引用文献

Morgan, H.P.,McNae, I.W.,Nowicki, M.W.,Hannaert, V.,Michels, P.A.M.,Fothergill-Gilmore, L.A.,Walkinshaw, M.D.
The allosteric mechanism of pryuvate kinase from Leishmania mexicana: a rock and lock model
J.Biol.Chem., 285:12892-12898, 2010

PubMed Abstract: Allosteric regulation provides a rate management system for enzymes involved in many cellular processes. Ligand-controlled regulation is easily recognizable, but the underlying molecular mechanisms have remained elusive. We have obtained the first complete series of allosteric structures, in all possible ligated states, for the tetrameric enzyme, pyruvate kinase, from Leishmania mexicana. The transition between inactive T-state and active R-state is accompanied by a simple symmetrical 6 degrees rigid body rocking motion of the A- and C-domain cores in each of the four subunits. However, formation of the R-state in this way is only part of the mechanism; eight essential salt bridge locks that form across the C-C interface provide tetramer rigidity with a coupled 7-fold increase in rate. The results presented here illustrate how conformational changes coupled with effector binding correlate with loss of flexibility and increase in thermal stability providing a general mechanism for allosteric control.

PubMed: 20123988
DOI: 10.1074/jbc.M109.079905

実験手法

X-RAY DIFFRACTION (2.3 Å)