1dfg: Difference between revisions

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[[Image:1dfg.~~jpg~~|left|200px]]

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

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~~==Overview==~~

Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.

==About this Structure==

1DFG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1DFG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFG OCA].

~~==Reference==~~

A mechanism of drug action revealed by structural studies of enoyl reductase., Baldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW, Science. 1996 Dec 20;274(5295):2107-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8953047 8953047]

[[Category: Escherichia coli]]

[[Category: Fatty Acid Synthase]]

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[[Category: Lipid biosynthesis]]

[[Category: Oxidoreductase]]

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-[[Image:1dfg.jpg|left|200px]]
+[[Image:1dfg.png|left|200px]]
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-==Overview==
+{{ABSTRACT_8953047}}
-Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.
 ==About this Structure==
 DFG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1DFG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFG OCA].
-==Reference==
-A mechanism of drug action revealed by structural studies of enoyl reductase., Baldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW, Science. 1996 Dec 20;274(5295):2107-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8953047 8953047]
 [[Category: Escherichia coli]]
 [[Category: Fatty Acid Synthase]]
@@ Line 29: / Line 25: @@
 [[Category: Lipid biosynthesis]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:47:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:10:15 2008''