Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase
| Autor: | Andrew H.-J. Wang, Tzu-Ping Ko, Shan-Hsueh Yao, Cheng-Chung Lee, Yueh-Te Chan, Ya-Wen Chen |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification ATP synthase biology Stereochemistry General Chemical Engineering Regulator General Chemistry Crystal structure 010402 general chemistry 01 natural sciences 0104 chemical sciences lcsh:Chemistry 03 medical and health sciences Residue (chemistry) 030104 developmental biology Enzyme Farnesyl diphosphate synthase lcsh:QD1-999 chemistry biology.protein Transferase |
| Zdroj: | ACS Omega, Vol 2, Iss 3, Pp 930-936 (2017) |
| ISSN: | 2470-1343 |
| Popis: | Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. Z,Z-Farnesyl diphosphate (Z,Z-FPP), synthesized by Z,Z-farnesyl diphosphate synthase (zFPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated zFPS (ΔzFPS) was determined. Irregular products including lavandulyl diphosphate and an unknown compound were surprisingly found. Apart from the truncated N-terminus as a functional regulator, structure-based analysis and mutagenesis assays revealed a residue H103 in ΔzFPS as one of the key elements to this irregular function. A series of substrate-enzyme complex structures were obtained from ΔzFPS-H103Y by co-crystallizing with isopentenyl diphosphate, dimethylallyl thiolodiphosphate, or both. Various substrate-binding modes were revealed. The catalytic mechanisms of both the head-to-tail and head-to-middle reactions in ΔzFPS were proposed. Functional switch between the two mechanisms in this enzyme and the essential role played by the flexible C-terminus were elucidated as well. |
| Databáze: | OpenAIRE |
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