2L22

Mupirocin didomain ACP

2L22 の概要

• エントリーDOI: 10.2210/pdb2l22/pdb
• NMR情報: BMRB: 17111
• 分子名称: Mupirocin didomain Acyl Carrier Protein (1 entity in total)
• 機能のキーワード: acyl carrier protein, mupirocin, biosynthetic protein
• 由来する生物種: Pseudomonas fluorescens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23764.72

構造登録者

Dong, X.,Williams, C.,Crump, M.P.,Wattana-amorn, P. (登録日: 2010-08-10, 公開日: 2012-02-15, 最終更新日: 2024-05-01)

主引用文献

Haines, A.S.,Dong, X.,Song, Z.,Farmer, R.,Williams, C.,Hothersall, J.,Poskon, E.,Wattana-Amorn, P.,Stephens, E.R.,Yamada, E.,Gurney, R.,Takebayashi, Y.,Masschelein, J.,Cox, R.J.,Lavigne, R.,Willis, C.L.,Simpson, T.J.,Crosby, J.,Winn, P.J.,Thomas, C.M.,Crump, M.P.
A conserved motif flags acyl carrier proteins for beta-branching in polyketide synthesis.
Nat.Chem.Biol., 9:685-692, 2013

PubMed Abstract: Type I polyketide synthases often use programmed β-branching, via enzymes of a 'hydroxymethylglutaryl-CoA synthase (HCS) cassette', to incorporate various side chains at the second carbon from the terminal carboxylic acid of growing polyketide backbones. We identified a strong sequence motif in acyl carrier proteins (ACPs) where β-branching is known to occur. Substituting ACPs confirmed a correlation of ACP type with β-branching specificity. Although these ACPs often occur in tandem, NMR analysis of tandem β-branching ACPs indicated no ACP-ACP synergistic effects and revealed that the conserved sequence motif forms an internal core rather than an exposed patch. Modeling and mutagenesis identified ACP helix III as a probable anchor point of the ACP-HCS complex whose position is determined by the core. Mutating the core affects ACP functionality, whereas ACP-HCS interface substitutions modulate system specificity. Our method for predicting β-carbon branching expands the potential for engineering new polyketides and lays a basis for determining specificity rules.

PubMed: 24056399
DOI: 10.1038/nchembio.1342

実験手法

SOLUTION NMR