1w6f: Difference between revisions

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[[Image:1w6f.gif|left|200px]]
{{Seed}}
[[Image:1w6f.png|left|200px]]


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{{STRUCTURE_1w6f|  PDB=1w6f  |  SCENE=  }}  
{{STRUCTURE_1w6f|  PDB=1w6f  |  SCENE=  }}  


'''ARYLAMINE N-ACETYLTRANSFERASE FROM MYCOBACTERIUM SMEGMATIS WITH THE ANTI-TUBERCULAR DRUG ISONIAZID BOUND IN THE ACTIVE SITE.'''
===ARYLAMINE N-ACETYLTRANSFERASE FROM MYCOBACTERIUM SMEGMATIS WITH THE ANTI-TUBERCULAR DRUG ISONIAZID BOUND IN THE ACTIVE SITE.===




==Overview==
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Isoniazid is a frontline drug used in the treatment of tuberculosis (TB). Isoniazid is a prodrug, requiring activation in the mycobacterial cell by the catalase/peroxidase activity of the katG gene product. TB kills two million people every year and the situation is getting worse due to the increase in prevalence of HIV/AIDS and emergence of multidrug-resistant strains of TB. Arylamine N-acetyltransferase (NAT) is a drug-metabolizing enzyme (E.C. 2.1.3.5). NAT can acetylate isoniazid, transferring an acetyl group from acetyl coenzyme A onto the terminal nitrogen of the drug, which in its N-acetylated form is therapeutically inactive. The bacterium responsible for TB, Mycobacterium tuberculosis, contains and expresses the gene encoding the NAT protein. Isoniazid binds to the NAT protein from Salmonella typhimurium and we report here the mode of binding of isoniazid in the NAT enzyme from Mycobacterium smegmatis, closely related to the M. tuberculosis and S. typhimurium NAT enzymes. The mode of binding of isoniazid to M. smegmatis NAT has been determined using data collected from two distinct crystal forms. We can say with confidence that the observed mode of binding of isoniazid is not an artifact of the crystallization conditions used. The NAT enzyme is active in mycobacterial cells and we propose that isoniazid binds to the NAT enzyme in these cells. NAT activity in M. tuberculosis is likely therefore to modulate the degree of activation of isoniazid by other enzymes within the mycobacterial cell. The structure of NAT with isoniazid bound will facilitate rational drug design for anti-tubercular therapy.
The line below this paragraph, {{ABSTRACT_PUBMED_15722451}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15722451 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15722451}}


==About this Structure==
==About this Structure==
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[[Category: Sim, E.]]
[[Category: Sim, E.]]
[[Category: Nat,tuberculosis,acetyltransferase,transferase]]
[[Category: Nat,tuberculosis,acetyltransferase,transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:13:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:22:26 2008''

Revision as of 04:22, 29 July 2008

File:1w6f.png

Template:STRUCTURE 1w6f

ARYLAMINE N-ACETYLTRANSFERASE FROM MYCOBACTERIUM SMEGMATIS WITH THE ANTI-TUBERCULAR DRUG ISONIAZID BOUND IN THE ACTIVE SITE.

Template:ABSTRACT PUBMED 15722451

About this Structure

1W6F is a Single protein structure of sequence from Mycobacterium smegmatis. Full crystallographic information is available from OCA.

Reference

Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis., Sandy J, Holton S, Fullam E, Sim E, Noble M, Protein Sci. 2005 Mar;14(3):775-82. PMID:15722451

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