2ccd: Difference between revisions
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Revision as of 11:45, 30 October 2007
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CRYSTAL STRUCTURE OF THE CATALASE-PEROXIDASE (KATG) AND S315T MUTANT FROM MYCOBACTERIUM TUBERCULOSIS
OverviewOverview
Inhibition of the enzyme Mycobacterium tuberculosis InhA (enoyl-acyl, carrier protein reductase) due to formation of an isonicotinoyl-NAD adduct, (IN-NAD) from isoniazid (INH) and nicotinamide adenine dinucleotide, cofactor is considered central to the mode of action of INH, a first-line, treatment for tuberculosis infection. INH action against mycobacteria, requires catalase-peroxidase (KatG) function, and IN-NAD adduct formation, is catalyzed in vitro by M. tuberculosis KatG under a variety of, conditions, yet a physiologically relevant approach to the process has not, emerged that allows scrutiny of the mechanism and the origins of INH, resistance in the most prevalent drug-resistant strain bearing, KatG[S315T]. In this report, we describe how hydrogen peroxide, delivered, at very low ... [(full description)]
About this StructureAbout this Structure
2CCD is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with HEM as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant., Zhao X, Yu H, Yu S, Wang F, Sacchettini JC, Magliozzo RS, Biochemistry. 2006 Apr 4;45(13):4131-40. PMID:16566587
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