5kh4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Steptococcus pneumoniae Undecaprenyl pyrophosphate Synthase (UPPS) with FARNESYL DIPHOSPHATE== | |
| + | <StructureSection load='5kh4' size='340' side='right' caption='[[5kh4]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5kh4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KH4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene></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=5kh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kh4 OCA], [http://pdbe.org/5kh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kh4 RCSB], [http://www.ebi.ac.uk/pdbsum/5kh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kh4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ISPT_STRPN ISPT_STRPN]] Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Undecaprenyl pyrophosphate synthase (UppS) is an essential enzyme in bacterial cell wall synthesis. Here we report the discovery of Staphylococcus aureus UppS inhibitors from an Encoded Library Technology screen and demonstrate binding to the hydrophobic substrate site through cocrystallography studies. The use of bacterial strains with regulated uppS expression and inhibitor resistant mutant studies confirmed that the whole cell activity was the result of UppS inhibition, validating UppS as a druggable antibacterial target. | ||
| - | + | Discovery and Characterization of a Class of Pyrazole Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase.,Concha N, Huang J, Bai X, Benowitz A, Brady P, Grady LC, Kryn LH, Holmes D, Ingraham K, Jin Q, Pothier Kaushansky L, McCloskey L, Messer JA, O'Keefe H, Patel A, Satz AL, Sinnamon RH, Schneck J, Skinner SR, Summerfield J, Taylor A, Taylor JD, Evindar G, Stavenger RA J Med Chem. 2016 Jul 20. PMID:27379833<ref>PMID:27379833</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5kh4" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Concha, N O]] | ||
| + | [[Category: Bacterial]] | ||
| + | [[Category: Native]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Undecaprenyl s. pneumoniae]] | ||
| + | [[Category: Upp]] | ||
Revision as of 15:07, 26 July 2016
Crystal Structure of Steptococcus pneumoniae Undecaprenyl pyrophosphate Synthase (UPPS) with FARNESYL DIPHOSPHATE
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