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

Das, S. ; Kumar, P. ; Bhor, V. ; Surolia, A. ; Vijayan, M. (2005) Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis Acta Crystallographica Section F, 61 . pp. 65-67. ISSN 1744-3091

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Official URL: http://scripts.iucr.org/cgi-bin/paper?bw5066

Related URL: http://dx.doi.org/10.1107/S1744309104028040

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.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:Pantothenate Kinase
ID Code:53849
Deposited On:10 Aug 2011 09:35
Last Modified:18 May 2016 06:48

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