Open AccessA preliminary crystallographic analysis of the putative mevalonate diphosphate decarboxylase from Trypanosoma brucei
Author(s) -
Byres Emma,
Martin David M. A.,
Hunter William N.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105014594
Subject(s) - trypanosoma brucei , monoclinic crystal system , enzyme , isopentenyl pyrophosphate , pyrophosphate , biosynthesis , biochemistry , mevalonate pathway , cofactor , stereochemistry , chemistry , crystallography , biology , gene , crystal structure
Mevalonate diphosphate decarboxylase catalyses the last and least well characterized step in the mevalonate pathway for the biosynthesis of isopentenyl pyrophosphate, an isoprenoid precursor. A gene predicted to encode the enzyme from Trypanosoma brucei has been cloned, a highly efficient expression system established and a purification protocol determined. The enzyme gives monoclinic crystals in space group P 2 1 , with unit‐cell parameters a = 51.5, b = 168.7, c = 54.9 Å, β = 118.8°. A Matthews coefficient V M of 2.5 Å 3 Da −1 corresponds to two monomers, each approximately 42 kDa (385 residues), in the asymmetric unit with 50% solvent content. These crystals are well ordered and data to high resolution have been recorded using synchrotron radiation.