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

Das, Satyabrata and Kumar, Parimal and Bhor, Vikrant and Surolia, A and Vijayan, M (2005) Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61 (Part 1). pp. 65-67.

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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 $P3_{1}21$. 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.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Blackwell Publishing.
Keywords: pantothenate kinase
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 24 Oct 2005
Last Modified: 19 Sep 2010 04:20
URI: http://eprints.iisc.ernet.in/id/eprint/3884

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