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| | ==Structure of E.coli FabF(C163A) in complex with Platencin== | | ==Structure of E.coli FabF(C163A) in complex with Platencin== |
| - | <StructureSection load='3ho2' size='340' side='right' caption='[[3ho2]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3ho2' size='340' side='right'caption='[[3ho2]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ho2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HO2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ho2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HO2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N32:2,4-DIHYDROXY-3-({3-[(2S,4AS,8S,8AR)-8-METHYL-3-METHYLIDENE-7-OXO-1,3,4,7,8,8A-HEXAHYDRO-2H-2,4A-ETHANONAPHTHALEN-8-YL]PROPANOYL}AMINO)BENZOIC+ACID'>N32</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hnz|3hnz]], [[3ho9|3ho9]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N32:2,4-DIHYDROXY-3-({3-[(2S,4AS,8S,8AR)-8-METHYL-3-METHYLIDENE-7-OXO-1,3,4,7,8,8A-HEXAHYDRO-2H-2,4A-ETHANONAPHTHALEN-8-YL]PROPANOYL}AMINO)BENZOIC+ACID'>N32</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1095, fabF, fabJ, JW1081 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3ho2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho2 OCA], [https://pdbe.org/3ho2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ho2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ho2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ho2 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_II Beta-ketoacyl-[acyl-carrier-protein] synthase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.179 2.3.1.179] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ho2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho2 OCA], [http://pdbe.org/3ho2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ho2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ho2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ho2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FABF_ECOLI FABF_ECOLI]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. | + | [https://www.uniprot.org/uniprot/FABF_ECOLI FABF_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Parthasarathy, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Soisson, S M]] | + | [[Category: Parthasarathy G]] |
| - | [[Category: Acyltransferase]] | + | [[Category: Soisson SM]] |
| - | [[Category: Fabf]]
| + | |
| - | [[Category: Fatty acid biosynthesis]]
| + | |
| - | [[Category: Ketoacyl synthase]]
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| - | [[Category: Lipid synthesis]]
| + | |
| - | [[Category: Platencin]]
| + | |
| - | [[Category: Platensimycin]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
FABF_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Natural products continue to serve as one of the best sources for discovery of antibacterial agents as exemplified by the recent discoveries of platensimycin and platencin. Chemical modifications as well as discovery of congeners are the main sources for gaining knowledge of structure-activity relationship of natural products. Screening for congeners in the extracts of the fermentation broths of Streptomyces platensis led to the isolation of platencin A(1), a hydroxy congener of platencin. The hydroxylation of the tricyclic enone moiety negatively affected the antibacterial activity and appears to be consistent with the hydrophobic binding pocket of the FabF. Isolation, structure, enzyme-bound structure and activity of platencin A(1) and two other congeners have been described.
Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis.,Singh SB, Ondeyka JG, Herath KB, Zhang C, Jayasuriya H, Zink DL, Parthasarathy G, Becker JW, Wang J, Soisson SM Bioorg Med Chem Lett. 2009 Aug 15;19(16):4756-9. Epub 2009 Jun 17. PMID:19581087[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Singh SB, Ondeyka JG, Herath KB, Zhang C, Jayasuriya H, Zink DL, Parthasarathy G, Becker JW, Wang J, Soisson SM. Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis. Bioorg Med Chem Lett. 2009 Aug 15;19(16):4756-9. Epub 2009 Jun 17. PMID:19581087 doi:10.1016/j.bmcl.2009.06.061
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