Reference : Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, p...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16748
Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase
English
Mandelman, D. [> > > >]
Bentahir, M. [> > > >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
Gerday, Colette [Centre Hospitalier Universitaire de Liège - CHU > > Gynécologie-Obstétrique CHR >]
Haser, R. [> > > >]
2001
Acta Crystallographica Section D-Biological Crystallography
Blackwell Publishing
57
Pt 11
1666-8
Yes (verified by ORBi)
International
0907-4449
Oxford
United Kingdom
[en] Crystallization ; Crystallography, X-Ray ; Phosphoglycerate Kinase/*chemistry ; Protein Conformation ; Pseudomonas/*enzymology ; Support, Non-U.S. Gov't
[en] 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.
http://hdl.handle.net/2268/16748

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