4C4R

Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride

4C4R の概要

• エントリーDOI: 10.2210/pdb4c4r/pdb
• 関連するPDBエントリー: 4C4S 4C4T
• 分子名称: BETA-PHOSPHOGLUCOMUTASE, MAGNESIUM ION, (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol, ... (5 entities in total)
• 機能のキーワード: phosphoryl transfer, transition state, metal fluoride, mutase, isomerase
• 由来する生物種: LACTOCOCCUS LACTIS
• 細胞内の位置: Cytoplasm (Potential): P71447
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24603.36

構造登録者

Pellegrini, E.,Bowler, M.W. (登録日: 2013-09-09, 公開日: 2014-07-16, 最終更新日: 2023-12-20)

主引用文献

Jin, Y.,Bhattasali, D.,Pellegrini, E.,Forget, S.M.,Baxter, N.J.,Cliff, M.J.,Bowler, M.W.,Jakeman, D.L.,Blackburn, G.M.,Waltho, J.P.
Alpha-Fluorophosphonates Reveal How a Phosphomutase Conserves Transition State Conformation Over Hexose Recognition in its Two-Step Reaction.
Proc.Natl.Acad.Sci.USA, 111:12384-, 2014

PubMed Abstract: β-Phosphoglucomutase (βPGM) catalyzes isomerization of β-D-glucose 1-phosphate (βG1P) into D-glucose 6-phosphate (G6P) via sequential phosphoryl transfer steps using a β-D-glucose 1,6-bisphosphate (βG16BP) intermediate. Synthetic fluoromethylenephosphonate and methylenephosphonate analogs of βG1P deliver novel step 1 transition state analog (TSA) complexes for βPGM, incorporating trifluoromagnesate and tetrafluoroaluminate surrogates of the phosphoryl group. Within an invariant protein conformation, the β-D-glucopyranose ring in the βG1P TSA complexes (step 1) is flipped over and shifted relative to the G6P TSA complexes (step 2). Its equatorial hydroxyl groups are hydrogen-bonded directly to the enzyme rather than indirectly via water molecules as in step 2. The (C)O-P bond orientation for binding the phosphate in the inert phosphate site differs by ∼ 30° between steps 1 and 2. By contrast, the orientations for the axial O-Mg-O alignment for the TSA of the phosphoryl group in the catalytic site differ by only ∼ 5°, and the atoms representing the five phosphorus-bonded oxygens in the two transition states (TSs) are virtually superimposable. The conformation of βG16BP in step 1 does not fit into the same invariant active site for step 2 by simple positional interchange of the phosphates: the TS alignment is achieved by conformational change of the hexose rather than the protein.

PubMed: 25104750
DOI: 10.1073/PNAS.1402850111

実験手法

X-RAY DIFFRACTION (1.1 Å)