3WYI
Structure of S. aureus undecaprenyl diphosphate synthase
Summary for 3WYI
| Entry DOI | 10.2210/pdb3wyi/pdb |
| Related | 3WYJ |
| Descriptor | Isoprenyl transferase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | isopentenyl diphosphate binding, product inhibition, transferase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 29950.81 |
| Authors | Gao, J.,Ko, T.P.,Huang, C.H.,Oldfield, E.,Guo, R.T. (deposition date: 2014-08-29, release date: 2015-02-04, Last modification date: 2023-11-08) |
| Primary citation | Zhu, W.,Wang, Y.,Li, K.,Gao, J.,Huang, C.H.,Chen, C.C.,Ko, T.P.,Zhang, Y.,Guo, R.T.,Oldfield, E. Antibacterial drug leads: DNA and enzyme multitargeting. J.Med.Chem., 58:1215-1227, 2015 Cited by PubMed Abstract: 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 °C. Several compounds also inhibited undecaprenyl diphosphate synthase (UPPS) with IC50 values of 100-500 nM, and we found good correlations (R(2) = 0.89, S. aureus; R(2) = 0.79, E. coli) between experimental and predicted cell growth inhibition by using DNA ΔTm 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. PubMed: 25574764DOI: 10.1021/jm501449u PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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