Open AccessCrystallization and preliminary X‐ray characterization of the glpX ‐encoded class II fructose‐1,6‐bisphosphatase from Mycobacterium tuberculosis
Author(s) -
Gutka Hiten J.,
Franzblau Scott G.,
Movahedzadeh Farahnaz,
AbadZapatero Cele
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111014722
Subject(s) - crystallization , mycobacterium tuberculosis , characterization (materials science) , class (philosophy) , chemistry , fructose , tuberculosis , crystallography , materials science , biochemistry , nanotechnology , organic chemistry , computer science , medicine , pathology , artificial intelligence
Fructose‐1,6‐bisphosphatase (FBPase; EC 3.1.3.11), which is a key enzyme in gluconeogenesis, catalyzes the hydrolysis of fructose 1,6‐bisphosphate to form fructose 6‐phosphate and orthophosphate. The present investigation reports the crystallization and preliminary crystallographic studies of the glpX ‐encoded class II FBPase from Mycobacterium tuberculosis H37Rv. The recombinant protein, which was cloned using an Escherichia coli expression system, was purified and crystallized using the hanging‐drop vapor‐diffusion method. The crystals diffracted to a resolution of 2.7 Å and belonged to the hexagonal space group P 6 1 22, with unit‐cell parameters a = b = 131.3, c = 143.2 Å. The structure has been solved by molecular replacement and is currently undergoing refinement.