1zid
From Proteopedia
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Activity: | [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR
Overview
The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in Mycobacterium tuberculosis. Despite the widespread use of this drug for more than 40 years, its precise mode of action has remained obscure. Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of InhA.
About this Structure
1ZID is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis., Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC, Science. 1998 Jan 2;279(5347):98-102. PMID:9417034 [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
Page seeded by OCA on Thu Mar 20 15:35:50 2008
Categories: Mycobacterium tuberculosis | Single protein | Jr., W R.Jacobs. | Rozwarski, D A. | Sacchettini, J C. | TBSGC, TB Structural Genomics Consortium. | ZID | Enoyl-acp reductase | Inha enzyme | Isoniazid | Modified nadh | Mycolic acid biosynthesis | Oxidoreductase | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Tuberculosis
