3vje: Difference between revisions

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-'''Unreleased structure'''
-The entry 3vje is ON HOLD
+==Crystal structure of the Y248A mutant of C(30) carotenoid dehydrosqualene synthase from Staphylococcus aureus in complex with zaragozic acid A==
+<StructureSection load='3vje' size='340' side='right'caption='[[3vje]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3vje]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VJE FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZGA:ZARAGOZIC+ACID+A'>ZGA</scene></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=3vje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vje OCA], [https://pdbe.org/3vje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vje RCSB], [https://www.ebi.ac.uk/pdbsum/3vje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vje ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CRTM_STAAU CRTM_STAAU]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Zaragozic acids (ZAs) belong to a family of fungal metabolites with nanomolar inhibitory activity toward squalene synthase (SQS). The enzyme catalyzes the committed step of sterol synthesis and has attracted attention as a potential target for antilipogenic and antiinfective therapies. Here, we have determined the structure of ZA-A complexed with human SQS. ZA-A binding induces a local conformational change in the substrate binding site, and its C-6 acyl group also extends over to the cofactor binding cavity. In addition, ZA-A effectively inhibits a homologous bacterial enzyme, dehydrosqualene synthase (CrtM), which synthesizes the precursor of staphyloxanthin in Staphylococcus aureus to cope with oxidative stress. Size reduction at Tyr(248) in CrtM further increases the ZA-A binding affinity, and it reveals a similar overall inhibitor binding mode to that of human SQS/ZA-A except for the C-6 acyl group. These structures pave the way for further improving selectivity and development of a new generation of anticholesterolemic and antimicrobial inhibitors.
-Authors: Liu, C.I., Jeng, W.Y., Chang, W.J., Wang, A.H.J.
+Binding modes of zaragozic acid A to human squalene synthase and staphylococcal dehydrosqualene synthase.,Liu CI, Jeng WY, Chang WJ, Ko TP, Wang AH J Biol Chem. 2012 May 25;287(22):18750-7. Epub 2012 Apr 3. PMID:22474324<ref>PMID:22474324</ref>
-Description: Crystal structure of the Y248A mutant of C(30) carotenoid dehydrosqualene synthase from Staphylococcus aureus in complex with zaragozic acid A
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3vje" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Squalene synthase|Squalene synthase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Staphylococcus aureus]]
+[[Category: Chang WJ]]
+[[Category: Jeng WY]]
+[[Category: Liu CI]]
+[[Category: Wang AHJ]]