1EE0

2-PYRONE SYNTHASE COMPLEXED WITH ACETOACETYL-COA

Summary for 1EE0

• Entry DOI: 10.2210/pdb1ee0/pdb
• Related: 1QLV
• Descriptor: 2-PYRONE SYNTHASE, ACETOACETYL-COENZYME A (3 entities in total)
• Functional Keywords: polyketide synthase, thiolase fold, transferase
• Biological source: Gerbera hybrid cultivar
• Total number of polymer chains: 2
• Total formula weight: 89370.21

Authors

Jez, J.M.,Austin, M.B.,Ferrer, J.,Bowmann, M.E.,Schroeder, J.,Noel, J.P. (deposition date: 2000-01-28, release date: 2001-01-31, Last modification date: 2011-07-13)

Primary citation

Jez, J.M.,Austin, M.B.,Ferrer, J.,Bowman, M.E.,Schroder, J.,Noel, J.P.
Structural control of polyketide formation in plant-specific polyketide synthases.
Chem.Biol., 7:919-930, 2000

PubMed Abstract: Polyketide synthases (PKSs) generate molecular diversity by utilizing different starter molecules and by controlling the final length of the polyketide. Although exploitation of this mechanistic variability has produced novel polyketides, the structural foundation of this versatility is unclear. Plant-specific PKSs are essential for the biosynthesis of anti-microbial phytoalexins, anthocyanin floral pigments, and inducers of Rhizobium nodulation genes. 2-Pyrone synthase (2-PS) and chalcone synthase (CHS) are plant-specific PKSs that share 74% amino acid sequence identity. 2-PS forms the triketide methylpyrone from an acetyl-CoA starter molecule and two malonyl-CoAs. CHS uses a p-coumaroyl-CoA starter molecule and three malonyl-CoAs to produce the tetraketide chalcone. Our goal was to elucidate the molecular basis of starter molecule selectivity and control of polyketide length in this class of PKS.

PubMed: 11137815
DOI: 10.1016/S1074-5521(00)00041-7

Experimental method

X-RAY DIFFRACTION (2.05 Å)