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Crystal structure of an IdeR-DNA complex reveals a conformational change in activated IdeR for base-specific interactions.
J Mol Biol
September 2004
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
The iron-dependent regulator (IdeR) is an essential protein in Mycobacterium tuberculosis that regulates iron uptake in this major pathogen. Under high iron concentrations, IdeR binds to several operator regions and represses transcription of target genes. Here, we report the first crystal structure of cobalt-activated IdeR bound to the mbtA-mbtB operator at 2.
View Article and Find Full Text PDFThe activities and isoenzyme pattern of cobalt-activated acylase and of aminoacylase I were estimated in carcinomas of bronchi, lung, thorax, stomach, colon and uterus. In all cancer tissues the activity of cobalt-activated acylase was markedly increased as compared with the normal tissue. Alterations of the isoenzyme pattern of cobalt-activated acylase were found in the carcinoma of stomach and of uterus, with the increased expression of the form-1 of the enzyme.
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