1mfp

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[[Image:1mfp.gif|left|200px]]
[[Image:1mfp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1mfp |SIZE=350|CAPTION= <scene name='initialview01'>1mfp</scene>, resolution 2.33&Aring;
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The line below this paragraph, containing "STRUCTURE_1mfp", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=IDN:(E)-N-METHYL-N-(1-METHYL-1H-INDOL-3-YLMETHYL)-3-(7-OXO-5,6,7,8-TETRAHYDRO-[1,8]NAPHTHYRIDIN-3-YL)-ACRYLAMIDE'>IDN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1mfp| PDB=1mfp | SCENE= }}
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|RELATEDENTRY=[[1c14|1C14]], [[1i2z|1I2Z]], [[1i30|1I30]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfp OCA], [http://www.ebi.ac.uk/pdbsum/1mfp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mfp RCSB]</span>
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}}
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'''E. coli Enoyl Reductase in complex with NAD and SB611113'''
'''E. coli Enoyl Reductase in complex with NAD and SB611113'''
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==Reference==
==Reference==
Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK., Seefeld MA, Miller WH, Newlander KA, Burgess WJ, DeWolf WE Jr, Elkins PA, Head MS, Jakas DR, Janson CA, Keller PM, Manley PJ, Moore TD, Payne DJ, Pearson S, Polizzi BJ, Qiu X, Rittenhouse SF, Uzinskas IN, Wallis NG, Huffman WF, J Med Chem. 2003 Apr 24;46(9):1627-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12699381 12699381]
Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK., Seefeld MA, Miller WH, Newlander KA, Burgess WJ, DeWolf WE Jr, Elkins PA, Head MS, Jakas DR, Janson CA, Keller PM, Manley PJ, Moore TD, Payne DJ, Pearson S, Polizzi BJ, Qiu X, Rittenhouse SF, Uzinskas IN, Wallis NG, Huffman WF, J Med Chem. 2003 Apr 24;46(9):1627-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12699381 12699381]
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[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
 
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Uzinskas, I N.]]
[[Category: Uzinskas, I N.]]
[[Category: Wallis, N G.]]
[[Category: Wallis, N G.]]
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[[Category: enoyl reductase]]
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[[Category: Enoyl reductase]]
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[[Category: enoyl-acp reductase]]
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[[Category: Enoyl-acp reductase]]
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[[Category: fabi]]
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[[Category: Fabi]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:58:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:15:39 2008''
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Revision as of 21:58, 2 May 2008

Image:1mfp.gif

Template:STRUCTURE 1mfp

E. coli Enoyl Reductase in complex with NAD and SB611113


Overview

Bacterial enoyl-ACP reductase (FabI) is responsible for catalyzing the final step of bacterial fatty acid biosynthesis and is an attractive target for the development of novel antibacterial agents. Previously we reported the development of FabI inhibitor 4 with narrow spectrum antimicrobial activity and in vivo efficacy against Staphylococcus aureus via intraperitoneal (ip) administration. Through iterative medicinal chemistry aided by X-ray crystal structure analysis, a new series of inhibitors has been developed with greatly increased potency against FabI-containing organisms. Several of these new inhibitors have potent antibacterial activity against multidrug resistant strains of S. aureus, and compound 30 demonstrates exceptional oral (po) in vivo efficacy in a S. aureus infection model in rats. While optimizing FabI inhibitory activity, compounds 29 and 30 were identified as having low micromolar FabK inhibitory activity, thereby increasing the antimicrobial spectrum of these compounds to include the FabK-containing pathogens Streptococcus pneumoniae and Enterococcus faecalis. The results described herein support the hypothesis that bacterial enoyl-ACP reductases are valid targets for antibacterial agents.

About this Structure

1MFP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK., Seefeld MA, Miller WH, Newlander KA, Burgess WJ, DeWolf WE Jr, Elkins PA, Head MS, Jakas DR, Janson CA, Keller PM, Manley PJ, Moore TD, Payne DJ, Pearson S, Polizzi BJ, Qiu X, Rittenhouse SF, Uzinskas IN, Wallis NG, Huffman WF, J Med Chem. 2003 Apr 24;46(9):1627-35. PMID:12699381 Page seeded by OCA on Sat May 3 00:58:32 2008

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