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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 61; no. 6; pp. 581 - 584
• Main Authors: Byres, Emma, Martin, David M. A., Hunter, William N.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.06.2005; International Union of Crystallography
• Subjects: Animals; Carboxy-Lyases - chemistry; Carboxy-Lyases - genetics; Carboxy-Lyases - isolation & purification; Cloning, Molecular; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; Crystallization; Crystallization Communications; CRYSTALS; decarboxylases; isoprenoids; mevalonate biosynthesis; MONOMERS; PRECURSOR; Protozoan Proteins - chemistry; Protozoan Proteins - genetics; Protozoan Proteins - isolation & purification; RESOLUTION; SOLVENTS; SPACE GROUPS; SYNCHROTRON RADIATION; Trypanosoma; Trypanosoma brucei brucei - enzymology; X-Ray Diffraction
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309105014594

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 P21, with unit‐cell parameters a = 51.5, b = 168.7, c = 54.9 Å, β = 118.8°. A Matthews coefficient VM of 2.5 Å3 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.