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 |
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Publication: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Publisher: | Blackwell Publishing |
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.ac.in/id/eprint/3884 |
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