5KH2
Crystal Structure of Steptococcus pneumoniae Undecaprenyl pyrophosphate Synthase (UPPS)
Summary for 5KH2
| Entry DOI | 10.2210/pdb5kh2/pdb |
| Related | 5KH4 5KH5 |
| Descriptor | Isoprenyl transferase (2 entities in total) |
| Functional Keywords | upps, native, bacterial, undecaprenyl s. pneumoniae, transferase |
| Biological source | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
| Total number of polymer chains | 4 |
| Total formula weight | 123644.82 |
| Authors | Concha, N.O. (deposition date: 2016-06-14, release date: 2016-07-20, Last modification date: 2024-03-06) |
| Primary citation | Concha, N.,Huang, J.,Bai, X.,Benowitz, A.,Brady, P.,Grady, L.C.,Kryn, L.H.,Holmes, D.,Ingraham, K.,Jin, Q.,Pothier Kaushansky, L.,McCloskey, L.,Messer, J.A.,O'Keefe, H.,Patel, A.,Satz, A.L.,Sinnamon, R.H.,Schneck, J.,Skinner, S.R.,Summerfield, J.,Taylor, A.,Taylor, J.D.,Evindar, G.,Stavenger, R.A. Discovery and Characterization of a Class of Pyrazole Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase. J.Med.Chem., 59:7299-7304, 2016 Cited by PubMed Abstract: 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. PubMed: 27379833DOI: 10.1021/acs.jmedchem.6b00746 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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