Qamra, R. and Prakash, P. and Aruna, B. and Hasnain, S.E. and Mande, S.C. (2005) Crystallization and preliminary X-ray crystallographic studies ofMycobacterium tuberculosischorismate mutase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 61 (5). pp. 473-475. ISSN 1744-3091

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Abstract

Chorismate mutase catalyzes the first committed step in the biosynthesis of the aromatic amino acids phenylalanine and tyrosine in bacteria, fungi and higher plants. The recent re-annotation of the Mycobacterium tuberculosis genome has revealed the presence of a duplicate set of genes coding for chorismate mutase. The mycobacterial gene Rv1885c bears <20% sequence homology to other bacterial chorismate mutases, thus serving as a potential target for the development of inhibitors specific to the pathogen. The M. tuberculosis chorismate mutase was crystallized in space group C2 and the crystals diffracted to a resolution of 2.2 Å. Matthews coefficient and self-rotation function calculations revealed the presence of two monomers in the asymmetric unit.

Item Type:	Article
Depositing User:	Users 2 not found.
Date Deposited:	15 Jul 2015 07:10
Last Modified:	15 Jul 2015 07:10
URI:	http://cdfd.sciencecentral.in/id/eprint/250

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