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

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...

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Bibliographic Details
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
Description
Summary: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.

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