2ied

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[[Image:2ied.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2ied| PDB=2ied | SCENE= }}
{{STRUCTURE_2ied| PDB=2ied | SCENE= }}
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'''CRYSTAL STRUCTURE of ISONIAZID-RESISTANT S94A ENOYL-ACP(COA) REDUCTASE MUTANT ENZYME FROM MYCOBACTERIUM TUBERCULOSIS UNCOMPLEXED'''
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===CRYSTAL STRUCTURE of ISONIAZID-RESISTANT S94A ENOYL-ACP(COA) REDUCTASE MUTANT ENZYME FROM MYCOBACTERIUM TUBERCULOSIS UNCOMPLEXED===
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==Overview==
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The resumption of tuberculosis led to an increased need to understand the molecular mechanisms of drug action and drug resistance, which should provide significant insight into the development of newer compounds. Isoniazid (INH), the most prescribed drug to treat TB, inhibits an NADH-dependent enoyl-acyl carrier protein reductase (InhA) that provides precursors of mycolic acids, which are components of the mycobacterial cell wall. InhA is the major target of the mode of action of isoniazid. INH is a pro-drug that needs activation to form the inhibitory INH-NAD adduct. Missense mutations in the inhA structural gene have been identified in clinical isolates of Mycobacterium tuberculosis resistant to INH. To understand the mechanism of resistance to INH, we have solved the structure of two InhA mutants (I21V and S94A), identified in INH-resistant clinical isolates, and compare them to INH-sensitive WT InhA structure in complex with the INH-NAD adduct. We also solved the structure of unliganded INH-resistant S94A protein, which is the first report on apo form of InhA. The salient features of these structures are discussed and should provide structural information to improve our understanding of the mechanism of action of, and resistance to, INH in M. tuberculosis. The unliganded structure of InhA allows identification of conformational changes upon ligand binding and should help structure-based drug design of more potent antimycobacterial agents.
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(as it appears on PubMed at http://www.pubmed.gov), where 17588773 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17588773}}
==About this Structure==
==About this Structure==
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[[Category: Inha reductase]]
[[Category: Inha reductase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:24:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:25:52 2008''

Revision as of 21:26, 27 July 2008

Image:2ied.png

Template:STRUCTURE 2ied

CRYSTAL STRUCTURE of ISONIAZID-RESISTANT S94A ENOYL-ACP(COA) REDUCTASE MUTANT ENZYME FROM MYCOBACTERIUM TUBERCULOSIS UNCOMPLEXED

Template:ABSTRACT PUBMED 17588773

About this Structure

2IED is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis., Dias MV, Vasconcelos IB, Prado AM, Fadel V, Basso LA, de Azevedo WF Jr, Santos DS, J Struct Biol. 2007 Sep;159(3):369-80. Epub 2007 May 3. PMID:17588773

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