9DU5

Cryo-EM structure of phosphoglucomutase from Thermococcus kodakarensis

9DU5 の概要

• エントリーDOI: 10.2210/pdb9du5/pdb
• EMDBエントリー: 47167
• 分子名称: Phosphoglucomutase/phosphomannomutase (1 entity in total)
• 機能のキーワード: isomerase, phosphotransferase activity, glycogen metabolism, thermococcus kodakarensis
• 由来する生物種: Thermococcus kodakarensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 199688.19

構造登録者

Naz, Z.,Rathore, I.,Saleem, M.,Rahman, M.,Rashid, N.,Wlodawer, A. (登録日: 2024-10-02, 公開日: 2025-04-16)

主引用文献

Naz, Z.,Rathore, I.,Saleem, M.,Rahman, M.,Wlodawer, A.,Rashid, N.
A Bifunctional Phosphoglucomutase/Phosphomannomutase from Thermococcus kodakarensis : Biophysical Analysis and Cryo-EM Structure.
Biomolecules, 15:-, 2025

PubMed Abstract: Phosphoglucomutase (EC 5.4.2.2., PGM), a key enzyme of glycogenolysis and glycogenesis, catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate, whereas phosphomannomutase (EC 5.4.2.8., PMM) transfers the phosphate group from the 1' to the 6', or from the 6' to the 1' position in mannose phosphate. However, in the hyperthermophilic archaeon , a single gene, , encodes a protein with both PGM and PMM activities. Here, we report biophysical analysis and the 2.45 Å resolution cryo-EM structure of this novel enzyme. Our results demonstrate a specific arrangement of the four subunits in the quaternary structure, displaying a distinct catalytic cleft required for the bifunctional activity at extremely high temperatures. To the best of our knowledge, this is the first biophysical characterization and cryo-EM structure elucidation of a thermostable, bifunctional PGM/PMM.

PubMed: 40149855
DOI: 10.3390/biom15030319

実験手法

ELECTRON MICROSCOPY (2.45 Å)