1gn3: Difference between revisions
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Revision as of 16:10, 30 October 2007
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H145Q MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.
OverviewOverview
We have refined the X-ray structures of two site-directed mutants of the, iron-dependent superoxide dismutase (SOD) from Mycobacterium tuberculosis., These mutations which affect residue 145 in the enzyme (H145Q and H145E), were designed to alter its metal-ion specificity. This residue is either, Gln or His in homologous SOD enzymes and has previously been shown to play, a role in active-site interactions since its side-chain helps to, coordinate the metal ion via a solvent molecule which is thought to be a, hydroxide ion. The mutations were based on the observation that in the, closely homologous manganese dependent SOD from Mycobacterium leprae, the, only significant difference from the M. tuberculosis SOD within 10 A of, the metal-binding site is the substitution of Gln for His at ... [(full description)]
About this StructureAbout this Structure
1GN3 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with FE as [ligand]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Engineering a change in metal-ion specificity of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis-- X-ray structure analysis of site-directed mutants., Bunting K, Cooper JB, Badasso MO, Tickle IJ, Newton M, Wood SP, Zhang Y, Young D, Eur J Biochem. 1998 Feb 1;251(3):795-803. PMID:9490054
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