1zid: Difference between revisions

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[[Image:1zid.~~gif~~|left|200px]]

[[Image:1zid.png|left|200px]]

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

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

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_9417034}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9417034 is the PubMed ID number.

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==About this Structure==

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[[Category: Tbsgc]]

[[Category: Tuberculosis]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 17~~:39:44 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:48:58 2008''

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-[[Image:1zid.gif|left|200px]]
+{{Seed}}
+[[Image:1zid.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1zid|  PDB=1zid  |  SCENE=  }}
-'''LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9417034}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9417034 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9417034}}
 ==About this Structure==
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 [[Category: Tbsgc]]
 [[Category: Tuberculosis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:39:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:48:58 2008''