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Literature summary for 4.2.3.17 extracted from

  • Koeksal, M.; Jin, Y.; Coates, R.M.; Croteau, R.; Christianson, D.W.
    Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis (2011), Nature, 469, 116-120.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Taxus brevifolia

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structure of a truncation variant lacking the transit sequence and an additional 27 residues at the N-terminus, complexed with 13-aza-13,14-dihydrocopalyl diphosphate, at 1.82 A resolution, and 2-fluorogeranylgeranyl diphosphate, at 2.25 A resolution. The structure reveals a modular assembly of three alpha-helical domains. The C-terminal catalytic domain is a class I terpenoid cyclase, which binds and activates substrate GGPP with a three-metal ion cluster. The N-terminal domain and a third insertion domain together adopt the fold of a vestigial class II terpenoid cyclase Taxus brevifolia

Protein Variants

Protein Variants Comment Organism
additional information construction of truncation variant lacking the transit sequence and an additional 27 residues at the N-terminus, crystallization data Taxus brevifolia

Organism

Organism UniProt Comment Textmining
Taxus brevifolia Q41594
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Synonyms

Synonyms Comment Organism
taxadiene synthase 5
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Taxus brevifolia