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5IK0

Tobacco 5-epi-aristolochene synthase with FPP

Summary for 5IK0
Entry DOI10.2210/pdb5ik0/pdb
Related5IK6 5IK9 5IKA
Descriptor5-epi-aristolochene synthase, MAGNESIUM ION, FARNESYL DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsterpene synthase, teas, fpp, lyase
Biological sourceNicotiana tabacum (Common tobacco)
Cellular locationCytoplasm: Q40577
Total number of polymer chains1
Total formula weight63656.94
Authors
Koo, H.J.,Xu, Y.,Louie, G.V.,Bowman, M.,Noel, J.P. (deposition date: 2016-03-03, release date: 2016-10-05, Last modification date: 2024-03-06)
Primary citationKoo, H.J.,Vickery, C.R.,Xu, Y.,Louie, G.V.,O'Maille, P.E.,Bowman, M.,Nartey, C.M.,Burkart, M.D.,Noel, J.P.
Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants.
J.Antibiot., 69:524-533, 2016
Cited by
PubMed Abstract: The plant terpene synthase (TPS) family is responsible for the biosynthesis of a variety of terpenoid natural products possessing diverse biological functions. TPSs catalyze the ionization and, most commonly, rearrangement and cyclization of prenyl diphosphate substrates, forming linear and cyclic hydrocarbons. Moreover, a single TPS often produces several minor products in addition to a dominant product. We characterized the catalytic profiles of Hyoscyamus muticus premnaspirodiene synthase (HPS) and compared it with the profile of a closely related TPS, Nicotiana tabacum 5-epi-aristolochene synthase (TEAS). The profiles of two previously studied HPS and TEAS mutants, each containing nine interconverting mutations, dubbed HPS-M9 and TEAS-M9, were also characterized. All four TPSs were compared under varying temperature and pH conditions. In addition, we solved the X-ray crystal structures of TEAS and a TEAS quadruple mutant complexed with substrate and products to gain insight into the enzymatic features modulating product formation. These informative structures, along with product profiles, provide new insight into plant TPS catalytic promiscuity.
PubMed: 27328867
DOI: 10.1038/ja.2016.68
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

238268

数据于2025-07-02公开中

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