3F5H

Crystal structure of fused docking domains from PikAIII and PikAIV of the pikromycin polyketide synthase

3F5H の概要

• エントリーDOI: 10.2210/pdb3f5h/pdb
• 関連するPDBエントリー: 1pzr
• 分子名称: Type I polyketide synthase PikAIII, Type I polyketide synthase PikAIV fusion protein, SODIUM ION (3 entities in total)
• 機能のキーワード: docking domain, polyketide synthase, pikromycin, h2-t2, protein binding
• 由来する生物種: Streptomyces venezuelae; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15291.81

構造登録者

Buchholz, T.J.,Geders, T.W.,Bartley, F.E.,Reynolds, K.A.,Smith, J.L.,Sherman, D.H. (登録日: 2008-11-03, 公開日: 2009-01-27, 最終更新日: 2023-12-27)

主引用文献

Buchholz, T.J.,Geders, T.W.,Bartley, F.E.,Reynolds, K.A.,Smith, J.L.,Sherman, D.H.
Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains.
Acs Chem.Biol., 4:41-52, 2009

PubMed Abstract: Bacterial type I polyketide synthases (PKSs) assemble structurally diverse natural products of significant clinical value from simple metabolic building blocks. The synthesis of these compounds occurs in a processive fashion along a large multiprotein complex. Transfer of the acyl intermediate across interpolypeptide junctions is mediated, at least in large part, by N- and C-terminal docking domains. We report here a comprehensive analysis of the binding affinity and selectivity for the complete set of discrete docking domain pairs in the pikromycin and erythromycin PKS systems. Despite disconnection from their parent module, each cognate pair of docking domains retained exquisite binding selectivity. Further insights were obtained by X-ray crystallographic analysis of the PikAIII/PikAIV docking domain interface. This new information revealed a series of key interacting residues that enabled development of a structural model for the recently proposed H2-T2 class of polypeptides involved in PKS intermodular molecular recognition.

PubMed: 19146481
DOI: 10.1021/cb8002607

実験手法

X-RAY DIFFRACTION (1.75 Å)