Crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis chorismate mutase.
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 A. Matthews coefficient and self-rotation function calculations revealed the presence of two monomers in the asymmetric unit.
Qamra
Rohini
R
Centre for DNA Fingerprinting and Diagnostics, ECIL Road, Nacharam, Hyderabad 500076, India.
Prakash
Prachee
P
Aruna
Bandi
B
Hasnain
Seyed E
SE
Mande
Shekhar C
SC
D002826:Chorismate Mutase / Q000737:chemistry* / Q000378:metabolism; D002850:Chromatography, Gel / Q000379:methods; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D019897:Periplasm / Q000201:enzymology; D011302:Prephenate Dehydratase / Q000378:metabolism; D011303:Prephenate Dehydrogenase / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D011303:Prephenate Dehydrogenase; D011302:Prephenate Dehydratase; D002826:Chorismate Mutase