Open AccessCrystallization and preliminary X‐ray crystallographic studies of Mycobacterium tuberculosis chorismate mutase
Author(s) -
Qamra Rohini,
Prakash Prachee,
Aruna Bandi,
Hasnain Seyed E.,
Mande Shekhar C.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105009383
Subject(s) - chorismate mutase , mutase , shikimate pathway , mycobacterium tuberculosis , aromatic amino acids , biochemistry , phenylalanine , stereochemistry , chemistry , biology , crystallography , amino acid , gene , tuberculosis , medicine , pathology
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 C 2 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.