4e9u: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4e9u]] is a 1 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=4E9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RWY:2-(4-PHENOXYPHENOXY)ETHYL+THIOCYANATE'>RWY</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RWY:2-(4-PHENOXYPHENOXY)ETHYL+THIOCYANATE'>RWY</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=4e9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9u OCA], [https://pdbe.org/4e9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9u RCSB], [https://www.ebi.ac.uk/pdbsum/4e9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CRTM_STAAU CRTM_STAAU]]
+[https://www.uniprot.org/uniprot/CRTM_STAAU CRTM_STAAU]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We report X-ray crystallographic structures of three inhibitors bound to dehydrosqualene synthase from Staphylococcus aureus: 1 (BPH-651), 2 (WC-9), and 3 (SQ-109). Compound 2 binds to the S2 site with its -SCN group surrounded by four hydrogen bond donors. With 1, we report two structures: in both, the quinuclidine headgroup binds in the allylic (S1) site with the side chain in S2, but in the presence of PPi and Mg(2+), the quinuclidine's cationic center interacts with PPi and three Mg(2+), mimicking a transition state involved in diphosphate ionization. With 3, there are again two structures. In one, the geranyl side chain binds to either S1 or S2 and the adamantane headgroup binds to S1. In the second, the side chain binds to S2 while the headgroup binds to S1. These results provide structural clues for the mechanism and inhibition of the head-to-head prenyl transferases and should aid future drug design.
-Head-to-Head Prenyl Tranferases: Anti-Infective Drug Targets.,Lin FY, Liu YL, Li K, Cao R, Zhu W, Axelson J, Pang R, Oldfield E J Med Chem. 2012 May 10;55(9):4367-72. Epub 2012 May 1. PMID:22486710<ref>PMID:22486710</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4e9u" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Squalene synthase|Squalene synthase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>