6HXE

Crystal structure of psychrophilic phosphoglycerate kinase from Pseudomonas TACII18 in complex with 3-phosphoglycerate

6HXE の概要

• エントリーDOI: 10.2210/pdb6hxe/pdb
• 関連するPDBエントリー: 6I06
• 分子名称: Phosphoglycerate kinase, 3-PHOSPHOGLYCERIC ACID (3 entities in total)
• 機能のキーワード: complex, 3-phosphoglycerate, hinge binding, transferase
• 由来する生物種: Pseudomonas sp. 'TAC II 18'
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40453.26

構造登録者

Mandelman, D.,Haser, R.,Aghajari, N. (登録日: 2018-10-17, 公開日: 2019-06-12, 最終更新日: 2024-01-24)

主引用文献

Mandelman, D.,Ballut, L.,Wolff, D.A.,Feller, G.,Gerday, C.,Haser, R.,Aghajari, N.
Structural determinants increasing flexibility confer cold adaptation in psychrophilic phosphoglycerate kinase.
Extremophiles, 23:495-506, 2019

PubMed Abstract: Crystal structures of phosphoglycerate kinase (PGK) from the psychrophile Pseudomonas sp. TACII 18 have been determined at high resolution by X-ray crystallography methods and compared with mesophilic, thermophilic and hyperthermophilic counterparts. PGK is a two-domain enzyme undergoing large domain movements to catalyze the production of ATP from 1,3-biphosphoglycerate and ADP. Whereas the conformational dynamics sustaining the catalytic mechanism of this hinge-bending enzyme now seems rather clear, the determinants which underlie high catalytic efficiency at low temperatures of this psychrophilic PGK were unknown. The comparison of the three-dimensional structures shows that multiple (global and local) specific adaptations have been brought about by this enzyme. Together, these reside in an overall increased flexibility of the cold-adapted PGK thereby allowing a better accessibility to the active site, but also a potentially more disordered transition state of the psychrophilic enzyme, due to the destabilization of some catalytic residues.

PubMed: 31147836
DOI: 10.1007/s00792-019-01102-x

実験手法

X-RAY DIFFRACTION (2.1 Å)