Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis

Mohamed Rehan, Aisyah and Paterson, Neil G. and Baker, Edward N. and Squire, Christopher J. (2011) Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67 (10). pp. 1274-1277. ISSN 1744-3091

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Abstract

During cofactor F420 biosynthesis, the enzyme F420-[gamma]-glutamyl ligase (FbiB) catalyzes the addition of [gamma]-linked L-glutamate residues to form polyglutamylated F420 derivatives. In Mycobacterium tuberculosis, Rv3262 (FbiB) consists of two domains: an N-terminal domain from the F420 ligase superfamily and a C-terminal domain with sequence similarity to nitro-FMN reductase superfamily proteins. To characterize the role of the C-terminal domain of FbiB in polyglutamyl ligation, it has been purified and crystallized in an apo form. The crystals diffracted to 2.0 Å resolution using a synchrotron source and belonged to the tetragonal space group P41212 (or P43212), with unit-cell parameters a = b = 136.6, c = 101.7 Å, [alpha] = [beta] = [gamma] = 90°.

Item Type:	Article (Journal)
Additional Information:	4469/9893
Uncontrolled Keywords:	Mycobacterium tuberculosis; F420 biosynthesis; FbiB
Subjects:	Q Science > Q Science (General) Q Science > QH Natural history > QH301 Biology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button):	Kulliyyah of Science > Department of Biotechnology
Depositing User:	Ms Rosyidah Taju Rahim
Date Deposited:	18 Jan 2012 12:05
Last Modified:	25 Jun 2013 09:51
URI:	http://irep.iium.edu.my/id/eprint/9893

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