1ZID

LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR

Summary for 1ZID

• Entry DOI: 10.2210/pdb1zid/pdb
• Descriptor: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, ISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase, inha enzyme, isoniazid, modified nadh, enoyl-acp reductase, tuberculosis, mycolic acid biosynthesis, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 29162.08

Authors

Rozwarski, D.A.,Jacobs Jr., W.R.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 1997-03-25, release date: 1998-03-25, Last modification date: 2024-05-22)

Primary citation

Rozwarski, D.A.,Grant, G.A.,Barton, D.H.,Jacobs Jr., W.R.,Sacchettini, J.C.
Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
Science, 279:98-102, 1998

PubMed Abstract: 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.

PubMed: 9417034
DOI: 10.1126/science.279.5347.98

Experimental method

X-RAY DIFFRACTION (2.7 Å)