6YDJ

P146A variant of beta-phosphoglucomutase from Lactococcus lactis in complex with glucose 6-phosphate and trifluoromagnesate

6YDJ の概要

• エントリーDOI: 10.2210/pdb6ydj/pdb
• 分子名称: Beta-phosphoglucomutase, 6-O-phosphono-beta-D-glucopyranose, TRIFLUOROMAGNESATE, ... (8 entities in total)
• 機能のキーワード: transition-state analogue, cis-trans proline isomerization, allomorphy, phosphoryl transfer, isomerase
• 由来する生物種: Lactococcus lactis subsp. lactis (strain IL1403)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24740.45

構造登録者

Wood, H.P.,Cruz-Navarrete, F.A.,Baxter, N.J.,Trevitt, C.R.,Robertson, A.J.,Dix, S.R.,Hounslow, A.M.,Cliff, M.J.,Waltho, J.P. (登録日: 2020-03-20, 公開日: 2020-10-28, 最終更新日: 2024-01-24)

主引用文献

Wood, H.P.,Cruz-Navarrete, F.A.,Baxter, N.J.,Trevitt, C.R.,Robertson, A.J.,Dix, S.R.,Hounslow, A.M.,Cliff, M.J.,Waltho, J.P.
Allomorphy as a mechanism of post-translational control of enzyme activity.
Nat Commun, 11:5538-5538, 2020

PubMed Abstract: Enzyme regulation is vital for metabolic adaptability in living systems. Fine control of enzyme activity is often delivered through post-translational mechanisms, such as allostery or allokairy. β-phosphoglucomutase (βPGM) from Lactococcus lactis is a phosphoryl transfer enzyme required for complete catabolism of trehalose and maltose, through the isomerisation of β-glucose 1-phosphate to glucose 6-phosphate via β-glucose 1,6-bisphosphate. Surprisingly for a gatekeeper of glycolysis, no fine control mechanism of βPGM has yet been reported. Herein, we describe allomorphy, a post-translational control mechanism of enzyme activity. In βPGM, isomerisation of the K145-P146 peptide bond results in the population of two conformers that have different activities owing to repositioning of the K145 sidechain. In vivo phosphorylating agents, such as fructose 1,6-bisphosphate, generate phosphorylated forms of both conformers, leading to a lag phase in activity until the more active phosphorylated conformer dominates. In contrast, the reaction intermediate β-glucose 1,6-bisphosphate, whose concentration depends on the β-glucose 1-phosphate concentration, couples the conformational switch and the phosphorylation step, resulting in the rapid generation of the more active phosphorylated conformer. In enabling different behaviours for different allomorphic activators, allomorphy allows an organism to maximise its responsiveness to environmental changes while minimising the diversion of valuable metabolites.

PubMed: 33139716
DOI: 10.1038/s41467-020-19215-9

実験手法

X-RAY DIFFRACTION (1.04 Å)