9C3X

Crystal structure of biphenyl synthase from Malus domestica complexed with triketide-CoA mimetic

これはPDB形式変換不可エントリーです。

9C3X の概要

• エントリーDOI: 10.2210/pdb9c3x/pdb
• 分子名称: BIS3 biphenyl synthase, (3R)-butane-1,3-diol, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-{[2-(5-oxo-5-phenylpentanamido)ethyl]amino}propyl)amino]butyl dihydrogen diphosphate, ... (4 entities in total)
• 機能のキーワード: polyketide synthase, transferase, coa analog
• 由来する生物種: Malus domestica (apple)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88592.88

構造登録者

Re, R.N.,Noel, J.P.,Burkart, M.D. (登録日: 2024-06-02, 公開日: 2025-05-14, 最終更新日: 2025-05-21)

主引用文献

Re, R.N.,La Clair, J.J.,Noel, J.P.,Burkart, M.D.
Elucidating the Iterative Elongation Mechanism in a Type III Polyketide Synthase.
J.Am.Chem.Soc., 147:16705-16714, 2025

PubMed Abstract: Type III polyketide synthases (PKSs) have a much simpler three-dimensional architecture compared with their type I and type II counterparts, yet they catalyze iterative polyketide elongation to generate a myriad of products in plants, fungi, and eubacteria. Despite this mechanistic complexity occurring within a single active site, the mechanism by which type III PKSs stabilize and direct their highly reactive keto and enolate intermediates has yet to be fully understood. Here, we report the synthesis and deployment of stable polyketone CoA analogues for each putative intermediate involved in the biphenyl synthase (BIS) mechanism together with three high-resolution crystal structures of each in complex with BIS from . This set of structures reveals key mechanistic features that control the number of iterative elongation steps and that shape the static architectural features responsible for organization of a water-mediated hydrogen bonding network necessary for termination of the elongation reaction by an intramolecular aldol cyclization and production of the 3,5-dihydroxybiphenyl BIS product. Elucidating these protein-substrate interactions provides a foundation for using polyketone CoA analogues to further unravel the control mechanisms of PKS catalysis and gain the insight necessary for predictive engineering of these enzymes.

PubMed: 40312803
DOI: 10.1021/jacs.5c05635

実験手法

X-RAY DIFFRACTION (1.45 Å)