Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase

• Published in: Acta Crystallographica Section D Biological Crystallography
• Main Authors: Mandelman, D., Bentahir, M., Feller, Georges, Gerday, Colette, Haser, R.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Blackwell Publishing 2001
• Subjects: Crystallization; Crystallography; X-Ray; Phosphoglycerate Kinase/*chemistry; Protein Conformation; Pseudomonas/*enzymology; Support; Non-U.S. Gov't; Life sciences; Biochemistry; biophysics & molecular biology; Sciences du vivant; Biochimie; biophysique & biologie moléculaire; Antarc*; Antarctic
• Online Access: https://orbi.uliege.be/handle/2268/16748; https://doi.org/10.1107/S0907444901012069

peer reviewed The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the preliminary crystallization and structure solution of psychrophilic PGK in its native form and cocrystallized with 3-phosphoglyceric acid (3-PGA) and the ATP analogue adenylyl imidophosphate (AMP-PNP) is reported. The complexed form of PGK crystallized in 2-3 d at 290 K, whereas the native form of the enzyme required 8-12 months. Morphologically, both crystal forms are similar and X-ray diffraction experiments indicate that the crystals are isomorphous. The crystals diffracted to a resolution of 2.0 A and belong to the space group P3(2). with unit-cell parameters a = b = 58.5, c = 85.4 A.