3g0y: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='3g0y' size='340' side='right'caption='[[3g0y]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3g0y' size='340' side='right'caption='[[3g0y]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3g0y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G0Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[3g0y]] 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=3G0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G0Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P9A:3-({3-[(1S,4AS,6S,7S,9S,9AR)-1,6-DIMETHYL-2-OXODECAHYDRO-6,9-EPOXY-4A,7-METHANOBENZO[7]ANNULEN-1-YL]PROPANOYL}AMINO)-2,4-DIHYDROXYBENZOIC+ACID'>P9A</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]] 2.6&#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;'>[[2gfx|2gfx]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P9A:3-({3-[(1S,4AS,6S,7S,9S,9AR)-1,6-DIMETHYL-2-OXODECAHYDRO-6,9-EPOXY-4A,7-METHANOBENZO[7]ANNULEN-1-YL]PROPANOYL}AMINO)-2,4-DIHYDROXYBENZOIC+ACID'>P9A</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1095, fabF, fabJ, JW1081 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_II Beta-ketoacyl-[acyl-carrier-protein] synthase II], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3g0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g0y OCA], [https://pdbe.org/3g0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g0y RCSB], [https://www.ebi.ac.uk/pdbsum/3g0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g0y 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=3g0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g0y OCA], [https://pdbe.org/3g0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g0y RCSB], [https://www.ebi.ac.uk/pdbsum/3g0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g0y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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]]
Line 38: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Parthasarathy, G]]
[[Category: Parthasarathy G]]
[[Category: Soisson, S M]]
[[Category: Soisson SM]]
[[Category: Acyltransferase]]
[[Category: Antibiotic]]
[[Category: Fatty acid biosynthesis]]
[[Category: Ketoacyl synthase]]
[[Category: Lipid synthesis]]
[[Category: Transferase]]

Latest revision as of 09:55, 6 September 2023

Structure of E. coli FabF(C163Q) in complex with dihydroplatensimycinStructure of E. coli FabF(C163Q) in complex with dihydroplatensimycin

Structural highlights

3g0y is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Platensimycin (1) displays antibacterial activity due to its inhibition of the elongation condensing enzyme (FabF), a novel mode of action that could potentially lead to a breakthrough in developing a new generation of antibiotics. The medicinal chemistry efforts were focused on the modification of the enone moiety of platensimycin and several analogs showed significant activity against FabF and possess antibacterial activity.

Synthesis and biological evaluation of platensimycin analogs.,Shen HC, Ding FX, Singh SB, Parthasarathy G, Soisson SM, Ha SN, Chen X, Kodali S, Wang J, Dorso K, Tata JR, Hammond ML, Maccoss M, Colletti SL Bioorg Med Chem Lett. 2009 Mar 15;19(6):1623-7. Epub 2009 Feb 7. PMID:19233644[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Shen HC, Ding FX, Singh SB, Parthasarathy G, Soisson SM, Ha SN, Chen X, Kodali S, Wang J, Dorso K, Tata JR, Hammond ML, Maccoss M, Colletti SL. Synthesis and biological evaluation of platensimycin analogs. Bioorg Med Chem Lett. 2009 Mar 15;19(6):1623-7. Epub 2009 Feb 7. PMID:19233644 doi:S0960-894X(09)00148-6

3g0y, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA