Open AccessCrystallization and preliminary X‐ray crystallographic analysis of MbtI, a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis
Author(s) -
Harrison Anthony J.,
Ramsay Rochelle J.,
Baker Edward N.,
Lott J. Shaun
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104031215
Subject(s) - siderophore , biosynthesis , crystallization , mycobacterium tuberculosis , microbiology and biotechnology , escherichia coli , tuberculosis , chemistry , secretion , bacteria , virulence , enzyme , stereochemistry , biochemistry , crystallography , biology , organic chemistry , medicine , gene , genetics , pathology
Mycobacterium tuberculosis , the causative agent of tuberculosis, depends on the secretion of salicylate‐based siderophores called mycobactins for the acquisition of extracellular iron, which is essential for the growth and virulence of the bacterium. The protein MbtI is thought to be the isochorismate synthase enzyme responsible for the conversion of chorismate to isochorismate, the first step in the salicylate production required for mycobactin biosynthesis. MbtI has been overexpressed in Escherichia coli , purified and crystallized. The crystals diffract to a maximum resolution of 1.8 Å. They belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 51.8, b = 163.4, c = 194.9 Å, consistent with the presence of either two, three or four molecules in the asymmetric unit.