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3u0f
From Proteopedia
(Difference between revisions)
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==The structure of Beta-ketoacyl synthase from Brucella melitensis bound to the fragment 7-hydroxycoumarin== | ==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]] 1.25Å' scene=''> | + | <StructureSection load='3u0f' size='340' side='right'caption='[[3u0f]], [[Resolution|resolution]] 1.25Å' scene=''> |
== Structural highlights == | == 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> | <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> | <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> | </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> | ||
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| + | From MEDLINE®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Brua2]] | [[Category: Brua2]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Beta-ketoacyl synthase]] | [[Category: Beta-ketoacyl synthase]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 06:18, 21 August 2019
The structure of Beta-ketoacyl synthase from Brucella melitensis bound to the fragment 7-hydroxycoumarin
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