Open AccessExpression, purification, crystallization and preliminary X‐ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis
Author(s) -
Das Satyabrata,
Kumar Parimal,
Bhor Vikrant,
Surolia A.,
Vijayan M.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104028040
Subject(s) - crystallization , enzyme , mycobacterium tuberculosis , cofactor , crystal (programming language) , protein subunit , coenzyme a , crystallography , chemistry , kinase , resolution (logic) , biochemistry , tuberculosis , reductase , gene , organic chemistry , medicine , pathology , computer science , programming language , artificial intelligence
Pantothenate kinase is an essential enzyme in the bacterial life cycle. It catalyzes the phosphorylation of pantothenate (vitamin B 5 ) 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 P 3 1 21. 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.