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Extremophiles

, Volume 23, Issue 5, pp 495–506 | Cite as

Structural determinants increasing flexibility confer cold adaptation in psychrophilic phosphoglycerate kinase

  • David Mandelman
  • Lionel Ballut
  • David A. Wolff
  • Georges Feller
  • Charles Gerday
  • Richard Haser
  • Nushin AghajariEmail author
Original Paper

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.

Keywords

Phosphoglycerate kinase Psychrophile Enzyme Hinge bending Pseudomonas sp. TACII 18 Cold adaptation 

Abbreviations

PGK

Phosphoglycerate kinase

3-PG

3-phosphoglycerate

1,3-PG

1,3-bisphosphoglycerate

AMP-PNP

Adenylyl imidophosphate

Notes

Acknowledgements

This work was supported by the Centre National de la Recherche Scientifique, by the European Union under the form of a TMR contract CT970131 (ColdNet), and by the Fonds National de la Recherche Scientifique, Belgium (Grants to GF and CG).

Supplementary material

792_2019_1102_MOESM1_ESM.pdf (666 kb)
Supplementary material 1 (PDF 667 kb)

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Copyright information

© Springer Japan KK, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Biocrystallography and Structural Biology of Therapeutic Targets, Molecular Microbiology and Structural BiochemistryUMR 5086, CNRS, University of Lyon 1Lyon Cedex 07France
  2. 2.Laboratory of Biochemistry, Center for Protein Engineering - InBioS, Institute of Chemistry B6aUniversity of LiègeLiègeBelgium

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