1BQ6
CHALCONE SYNTHASE FROM ALFALFA WITH COENZYME A
1BQ6 の概要
エントリーDOI | 10.2210/pdb1bq6/pdb |
分子名称 | CHALCONE SYNTHASE, SULFATE ION, COENZYME A, ... (4 entities in total) |
機能のキーワード | transferase, polyketide synthase, chalcone biosynthesis |
由来する生物種 | Medicago sativa |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 43519.68 |
構造登録者 | Ferrer, J.-L.,Bowman, M.E.,Jez, J.,Dixon, R.,Noel, J.P. (登録日: 1998-08-21, 公開日: 1999-08-11, 最終更新日: 2024-10-16) |
主引用文献 | Ferrer, J.L.,Jez, J.M.,Bowman, M.E.,Dixon, R.A.,Noel, J.P. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat.Struct.Biol., 6:775-784, 1999 Cited by PubMed Abstract: Chalcone synthase (CHS) is pivotal for the biosynthesis of flavonoid antimicrobial phytoalexins and anthocyanin pigments in plants. It produces chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A thioesters into a polyketide reaction intermediate that cyclizes. The crystal structures of CHS alone and complexed with substrate and product analogs reveal the active site architecture that defines the sequence and chemistry of multiple decarboxylation and condensation reactions and provides a molecular understanding of the cyclization reaction leading to chalcone synthesis. The structure of CHS complexed with resveratrol also suggests how stilbene synthase, a related enzyme, uses the same substrates and an alternate cyclization pathway to form resveratrol. By using the three-dimensional structure and the large database of CHS-like sequences, we can identify proteins likely to possess novel substrate and product specificity. The structure elucidates the chemical basis of plant polyketide biosynthesis and provides a framework for engineering CHS-like enzymes to produce new products. PubMed: 10426957DOI: 10.1038/11553 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.56 Å) |
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