A preliminary crystallographic analysis of the putative mevalonate diphosphate decarboxylase from Trypanosoma brucei

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt 6):581-4. doi: 10.1107/S1744309105014594. Epub 2005 Jun 1.

Abstract

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 P2(1), with unit-cell parameters a = 51.5, b = 168.7, c = 54.9 A, beta = 118.8 degrees. A Matthews coefficient VM of 2.5 A3 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carboxy-Lyases / chemistry*
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / isolation & purification
  • Cloning, Molecular
  • Crystallization
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / genetics
  • Protozoan Proteins / isolation & purification
  • Trypanosoma brucei brucei / enzymology*
  • X-Ray Diffraction

Substances

  • Protozoan Proteins
  • Carboxy-Lyases
  • pyrophosphomevalonate decarboxylase