5HXP
Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase (D71M, E75A and H103Y Mutants) Complexed with IPP
Summary for 5HXP
Entry DOI | 10.2210/pdb5hxp/pdb |
Related | 5HXN 5HXO 5HXQ 5HXT |
Descriptor | (2Z,6Z)-farnesyl diphosphate synthase, chloroplastic, ISOPENTYL PYROPHOSPHATE, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | prenyltransferase, transferase |
Biological source | Solanum habrochaites (Wild tomato) |
Total number of polymer chains | 2 |
Total formula weight | 54864.77 |
Authors | Lee, C.C.,Chan, Y.T.,Wang, A.H.J. (deposition date: 2016-01-31, release date: 2017-04-05, Last modification date: 2023-11-08) |
Primary citation | Chan, Y.T.,Ko, T.P.,Yao, S.H.,Chen, Y.W.,Lee, C.C.,Wang, A.H. Crystal Structure and Potential Head-to-Middle Condensation Function of aZ,Z-Farnesyl Diphosphate Synthase. Acs Omega, 2:930-936, 2017 Cited by PubMed Abstract: Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. ,-Farnesyl diphosphate (,-FPP), synthesized by ,-farnesyl diphosphate synthase (FPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated FPS (ΔFPS) 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 ΔFPS as one of the key elements to this irregular function. A series of substrate-enzyme complex structures were obtained from ΔFPS-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 ΔFPS 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. PubMed: 30023621DOI: 10.1021/acsomega.6b00562 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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