3wyj
From Proteopedia
(Difference between revisions)
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==Structure of E. coli undecaprenyl diphosphate synthase in complex with BPH-789== | ==Structure of E. coli undecaprenyl diphosphate synthase in complex with BPH-789== | ||
| - | <StructureSection load='3wyj' size='340' side='right'caption='[[3wyj]]' scene=''> | + | <StructureSection load='3wyj' size='340' side='right'caption='[[3wyj]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wyj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYJ FirstGlance]. <br> |
| - | </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=3wyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyj OCA], [https://pdbe.org/3wyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wyj RCSB], [https://www.ebi.ac.uk/pdbsum/3wyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wyj ProSAT]</span></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]] 2.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H78:[1-OXIDANYL-2-[3-[3-[[3-[[3-[3-(2-OXIDANYL-2,2-DIPHOSPHONO-ETHYL)PHENYL]PHENYL]SULFAMOYL]PHENYL]SULFONYLAMINO]PHENYL]PHENYL]-1-PHOSPHONO-ETHYL]PHOSPHONIC+ACID'>H78</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=3wyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyj OCA], [https://pdbe.org/3wyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wyj RCSB], [https://www.ebi.ac.uk/pdbsum/3wyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wyj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UPPS_ECOLI UPPS_ECOLI] Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.<ref>PMID:12756244</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We report the results of an investigation of the activity of a series of amidine and bisamidine compounds against Staphylococcus aureus and Escherichia coli. The most active compounds bound to an AT-rich DNA dodecamer (CGCGAATTCGCG)2 and using DSC were found to increase the melting transition by up to 24 degrees C. Several compounds also inhibited undecaprenyl diphosphate synthase (UPPS) with IC50 values of 100-500 nM, and we found good correlations (R2 = 0.89, S. aureus; R2 = 0.79, E. coli) between experimental and predicted cell growth inhibition by using DNA DeltaTm and UPPS IC50 experimental results together with one computed descriptor. We also solved the structures of three bisamidines binding to DNA as well as three UPPS structures. Overall, the results are of general interest in the context of the development of resistance-resistant antibiotics that involve multitargeting. | ||
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| + | Antibacterial Drug Leads: DNA and Enzyme Multitargeting.,Zhu W, Wang Y, Li K, Gao J, Huang CH, Chen CC, Ko TP, Zhang Y, Guo RT, Oldfield E J Med Chem. 2015 Jan 22. PMID:25574764<ref>PMID:25574764</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3wyj" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]] | *[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gao J]] | [[Category: Gao J]] | ||
Current revision
Structure of E. coli undecaprenyl diphosphate synthase in complex with BPH-789
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