1zid

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{{STRUCTURE_1zid| PDB=1zid | SCENE= }}
{{STRUCTURE_1zid| PDB=1zid | SCENE= }}
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'''LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR'''
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===LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9417034 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9417034}}
==About this Structure==
==About this Structure==
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[[Category: Tbsgc]]
[[Category: Tbsgc]]
[[Category: Tuberculosis]]
[[Category: Tuberculosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:48:58 2008''

Revision as of 16:49, 28 July 2008

Image:1zid.png

Template:STRUCTURE 1zid

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

Template:ABSTRACT PUBMED 9417034

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

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