6I06

Crystal structure of psychrophilic phosphoglycerate kinase from Pseudomonas TACII18

Summary for 6I06

• Entry DOI: 10.2210/pdb6i06/pdb
• Related: 6HXE
• Descriptor: Phosphoglycerate kinase (2 entities in total)
• Functional Keywords: hinge binding, transferase, kinase, glycolysis
• Biological source: Pseudomonas
• Total number of polymer chains: 1
• Total formula weight: 40302.25

Authors

Mandelman, D.,Haser, R.,Aghajari, N. (deposition date: 2018-10-25, release date: 2019-06-12, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)