5EAS
5-EPI-ARISTOLOCHENE SYNTHASE FROM NICOTIANA TABACUM
Summary for 5EAS
Entry DOI | 10.2210/pdb5eas/pdb |
Descriptor | 5-EPI-ARISTOLOCHENE SYNTHASE, MAGNESIUM ION (3 entities in total) |
Functional Keywords | isoprenoid synthase, isoprenoid cyclase, 5-epi-aristolochene synthase, isoprenoid biosynthesis, natural products biosynthesis |
Biological source | Nicotiana tabacum (common tobacco) |
Cellular location | Cytoplasm: Q40577 |
Total number of polymer chains | 1 |
Total formula weight | 63116.09 |
Authors | Starks, C.M.,Back, K.,Chappell, J.,Noel, J.P. (deposition date: 1997-06-19, release date: 1997-10-15, Last modification date: 2024-03-13) |
Primary citation | Starks, C.M.,Back, K.,Chappell, J.,Noel, J.P. Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase. Science, 277:1815-1820, 1997 Cited by PubMed Abstract: Terpene cyclases catalyze the synthesis of cyclic terpenes with 10-, 15-, and 20-carbon acyclic isoprenoid diphosphates as substrates. Plants have been a source of these natural products by providing a homologous set of terpene synthases. The crystal structures of 5-epi-aristolochene synthase, a sesquiterpene cyclase from tobacco, alone and complexed separately with two farnesyl diphosphate analogs were analyzed. These structures reveal an unexpected enzymatic mechanism for the synthesis of the bicyclic product, 5-epi-aristolochene, and provide a basis for understanding the stereochemical selectivity displayed by other cyclases in the biosynthesis of pharmacologically important cyclic terpenes. As such, these structures provide templates for the engineering of novel terpene cyclases. PubMed: 9295271DOI: 10.1126/science.277.5333.1815 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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