3hnz
From Proteopedia
(Difference between revisions)
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<StructureSection load='3hnz' size='340' side='right'caption='[[3hnz]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='3hnz' size='340' side='right'caption='[[3hnz]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3hnz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3hnz]] 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=3HNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HNZ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMN:PLATENSIMYCIN'>PMN</scene></td></tr> | |
- | <tr id=' | + | |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hnz OCA], [https://pdbe.org/3hnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hnz RCSB], [https://www.ebi.ac.uk/pdbsum/3hnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hnz 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=3hnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hnz OCA], [https://pdbe.org/3hnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hnz RCSB], [https://www.ebi.ac.uk/pdbsum/3hnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hnz 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. | |
== 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=3hnz 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=3hnz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == 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. | ||
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- | 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<ref>PMID:19581087</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3hnz" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Parthasarathy | + | [[Category: Parthasarathy G]] |
- | [[Category: Soisson | + | [[Category: Soisson SM]] |
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Current revision
Structure of E. coli FabF(C163A) in Complex with Platensimycin
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