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5HXP

Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase (D71M, E75A and H103Y Mutants) Complexed with IPP

Summary for 5HXP
Entry DOI10.2210/pdb5hxp/pdb
Related5HXN 5HXO 5HXQ 5HXT
Descriptor(2Z,6Z)-farnesyl diphosphate synthase, chloroplastic, ISOPENTYL PYROPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsprenyltransferase, transferase
Biological sourceSolanum habrochaites (Wild tomato)
Total number of polymer chains2
Total formula weight54864.77
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 citationChan, 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: 30023621
DOI: 10.1021/acsomega.6b00562
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

243083

数据于2025-10-15公开中

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