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==Crystal structure of beta-ketoacyl synthase from Brucella melitensis in complex with platencin==
==Crystal structure of beta-ketoacyl synthase from Brucella melitensis in complex with platencin==
<StructureSection load='4jv3' size='340' side='right'caption='[[4jv3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4jv3' size='340' side='right'caption='[[4jv3]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jv3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JV3 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JV3 FirstGlance]. <br>
</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>
</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=4jv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jv3 OCA], [https://pdbe.org/4jv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jv3 RCSB], [https://www.ebi.ac.uk/pdbsum/4jv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jv3 ProSAT]</span></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lrf|3lrf]]</div></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_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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=4jv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jv3 OCA], [https://pdbe.org/4jv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jv3 RCSB], [https://www.ebi.ac.uk/pdbsum/4jv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jv3 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial fatty acid pathway is essential for membrane synthesis and a range of other metabolic and cellular functions. The beta-ketoacyl-ACP synthases carry out the initial elongation reaction of this pathway, utilizing acetyl-CoA as a primer to elongate malonyl-ACP by two carbons, and subsequent elongation of the fatty acyl-ACP substrate by two carbons. Here we describe the structures of the beta-ketoacyl-ACP synthase I from Brucella melitensis in complex with platencin, 7-hydroxycoumarin, and (5-thiophen-2-ylisoxazol-3-yl)methanol. The enzyme is a dimer and based on structural and sequence conservation, harbors the same active site configuration as other beta-ketoacyl-ACP synthases. The platencin binding site overlaps with the fatty acyl compound supplied by ACP, while 7-hydroxyl-coumarin and (5-thiophen-2-ylisoxazol-3-yl)methanol bind at the secondary fatty acyl binding site. These high-resolution structures, ranging between 1.25 and 1.70 a resolution, provide a basis for in silico inhibitor screening and optimization, and can aid in rational drug design by revealing the high-resolution binding interfaces of molecules at the malonyl-ACP and acyl-ACP active sites.
Structural characterization of beta-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites.,Patterson EI, Nanson JD, Abendroth J, Bryan C, Sankaran B, Myler PJ, Forwood JK Proteins. 2019 Jun 25. doi: 10.1002/prot.25765. PMID:31237717<ref>PMID:31237717</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jv3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Beta-ketoacyl synthase]]
[[Category: Platencin]]
[[Category: Ssgcid]]
[[Category: Transferase-antibiotic complex]]
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