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| Home > Publications database > Protonation State and Hydration of Bisphosphonate Bound to Farnesyl Pyrophosphate Synthase |
| Home > Publications database > Protonation State and Hydration of Bisphosphonate Bound to Farnesyl Pyrophosphate Synthase |
| Journal Article | FZJ-2015-06693 |
; ; ; ; ; ;
2015
ACS
Washington, DC
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Please use a persistent id in citations: doi:10.1021/acs.jmedchem.5b01147
Abstract: Farnesyl pyrophosphate synthase (FPPS) catalyzes the condensation of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate to FPP and is known to be a molecular target of osteoporosis drugs, such as risedronate (RIS), which is a nitrogen-containing bisphosphonate. The protonation states and hydration structure of RIS bound to FPPS were determined by neutron protein crystallography, which allows direct visualization of hydrogens and deuteriums. The structure analysis revealed that the phosphate groups of RIS were fully deprotonated with the abnormally decreased pKa, and that the roles of E93 and D264 consisted of canceling the extra negative charges upon the binding of ligands. Collectively, our neutron structures provided insights into the physicochemical properties during the bisphosphonate binding event.
Keyword(s): Health and Life (1st) ; Health and Life (1st) ; Biology (2nd) ; Crystallography (2nd)
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