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<StructureSection load='1mfp' size='340' side='right'caption='[[1mfp]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
<StructureSection load='1mfp' size='340' side='right'caption='[[1mfp]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mfp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MFP FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mfp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MFP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c14|1c14]], [[1i2z|1i2z]], [[1i30|1i30]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfp OCA], [https://pdbe.org/1mfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mfp RCSB], [https://www.ebi.ac.uk/pdbsum/1mfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mfp ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfp OCA], [https://pdbe.org/1mfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mfp RCSB], [https://www.ebi.ac.uk/pdbsum/1mfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mfp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FABI_ECOLI FABI_ECOLI]] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.<ref>PMID:8119879</ref> <ref>PMID:7592873</ref> <ref>PMID:20693992</ref>
[https://www.uniprot.org/uniprot/FABI_ECOLI FABI_ECOLI] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.<ref>PMID:8119879</ref> <ref>PMID:7592873</ref> <ref>PMID:20693992</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mfp ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mfp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12699381</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mfp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Burgess, W J]]
[[Category: Burgess WJ]]
[[Category: DeWolf, W E]]
[[Category: DeWolf Jr WE]]
[[Category: Elkins, P A]]
[[Category: Elkins PA]]
[[Category: Head, M S]]
[[Category: Head MS]]
[[Category: Huffman, W F]]
[[Category: Huffman WF]]
[[Category: Jakas, D R]]
[[Category: Jakas DR]]
[[Category: Janson, C A]]
[[Category: Janson CA]]
[[Category: Keller, P M]]
[[Category: Keller PM]]
[[Category: Manley, P J]]
[[Category: Manley PJ]]
[[Category: Miller, W H]]
[[Category: Miller WH]]
[[Category: Moore, T D]]
[[Category: Moore TD]]
[[Category: Newlander, K A]]
[[Category: Newlander KA]]
[[Category: Payne, D J]]
[[Category: Payne DJ]]
[[Category: Pearson, S]]
[[Category: Pearson S]]
[[Category: Polizzi, B J]]
[[Category: Polizzi BJ]]
[[Category: Qiu, X]]
[[Category: Qiu X]]
[[Category: Rittenhouse, S F]]
[[Category: Rittenhouse SF]]
[[Category: Seefeld, M A]]
[[Category: Seefeld MA]]
[[Category: Uzinskas, I N]]
[[Category: Uzinskas IN]]
[[Category: Wallis, N G]]
[[Category: Wallis NG]]
[[Category: Enoyl reductase]]
[[Category: Enoyl-acp reductase]]
[[Category: Fabi]]
[[Category: Oxidoreductase]]

Latest revision as of 07:43, 14 February 2024

E. coli Enoyl Reductase in complex with NAD and SB611113

1mfp, resolution 2.33Å

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