Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 1 (January 2005)

crystallization communications

Acta Cryst. (2005). F61, 65-67 [ doi:10.1107/S1744309104028040 ]

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis

S. Das, P. Kumar, V. Bhor, A. Surolia and M. Vijayan

Abstract: Pantothenate kinase is an essential enzyme in the bacterial life cycle. It catalyzes the phosphorylation of pantothenate (vitamin B₅) to 4'-phosphopantothenate, the first step in the coenzyme A biosynthetic pathway. The enzyme from Mycobacterium tuberculosis, MW 35.7 kDa, has been cloned, expressed, purified and crystallized in two different trigonal crystal forms, both belonging to space group P3₁21. Two complete data sets of resolution 2.5 Å (form I) and 2.9 Å (form II) from crystals with unit-cell parameters a = b = 78.3, c = 115.45 Å and a = b = 107.63, c = 89.85 Å, respectively, were collected at room temperature on a home X-ray source. Structures of both crystal forms were solved for one subunit in the asymmetric unit by molecular replacement.

Keywords: pantothenate kinase.