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-Structure paper
Title | The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates |
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Journal, issue, pages | TO BE PUBLISHED |
Publish date | Nov 1, 2013 (structure data deposition date) |
Authors | Tsoumpra, M.K. / Muniz, J.R.C. / Barnett, B.L. / Pilka, E. / Kwaasi, A.A. / Kavanagh, K.L. / Evdokimov, A. / Walter, R.L. / Ebetino, F.H. / Oppermann, U. ...Tsoumpra, M.K. / Muniz, J.R.C. / Barnett, B.L. / Pilka, E. / Kwaasi, A.A. / Kavanagh, K.L. / Evdokimov, A. / Walter, R.L. / Ebetino, F.H. / Oppermann, U. / Russell, R.G.G. / Dunford, J.E. |
External links | Search PubMed |
Methods | X-ray diffraction |
Resolution | 1.43 - 2.35 Å |
Structure data | PDB-4ng6: PDB-4nke: PDB-4nkf: PDB-4nua: PDB-4ogu: |
Chemicals | ChemComp-MG: ChemComp-IPE: ChemComp-RIS: ChemComp-HOH: ChemComp-EDO: ChemComp-210: ChemComp-PEG: ChemComp-PO4: |
Source |
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Keywords | TRANSFERASE / Alpha-Helical Prenyltransferase / Isoprene Biosynthesis / Lipid Synthesis / Steroid Biosynthesis / Isoprenoid Pathway / Cholesterol Synthesis / Bisphosphonates / Alpha-Helical Prenyltransferase Fold / Isoprene Synthesis / Dimethylallyl Pyrophosphate / Isopentenyl Pyrophosphate / All Alpha-Helical / Prenyltransferase / Lipid Biosynthesis |