3u0f: Difference between revisions

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 ==The structure of Beta-ketoacyl synthase from Brucella melitensis bound to the fragment 7-hydroxycoumarin==
-<StructureSection load='3u0f' size='340' side='right' caption='[[3u0f]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
+<StructureSection load='3u0f' size='340' side='right'caption='[[3u0f]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3u0f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brua2 Brua2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U0F FirstGlance]. <br>
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 <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=3u0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u0f OCA], [http://pdbe.org/3u0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u0f RCSB], [http://www.ebi.ac.uk/pdbsum/3u0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u0f ProSAT]</span></td></tr>
 </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 3u0f" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Brua2]]
+[[Category: Large Structures]]
 [[Category: Structural genomic]]
 [[Category: Beta-ketoacyl synthase]]
 [[Category: Ssgcid]]
 [[Category: Transferase]]