6DFL

WaaP in complex with acyl carrier protein

6DFL の概要

• エントリーDOI: 10.2210/pdb6dfl/pdb
• 分子名称: Lipopolysaccharide core heptose(I) kinase RfaP, Acyl carrier protein, S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] hexadecanethioate (3 entities in total)
• 機能のキーワード: bacterial sugar kinase, hydrolase
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39146.78

構造登録者

Chopra, R.,Vash, B. (登録日: 2018-05-15, 公開日: 2019-04-03, 最終更新日: 2024-11-06)

主引用文献

Kreamer, N.N.K.,Chopra, R.,Caughlan, R.E.,Fabbro, D.,Fang, E.,Gee, P.,Hunt, I.,Li, M.,Leon, B.C.,Muller, L.,Vash, B.,Woods, A.L.,Stams, T.,Dean, C.R.,Uehara, T.
Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase.
Sci Rep, 8:14124-14124, 2018

PubMed Abstract: Phosphorylation of Pseudomonas aeruginosa lipopolysaccharide (LPS) is important for maintaining outer membrane integrity and intrinsic antibiotic resistance. We solved the crystal structure of the LPS heptose kinase WaaP, which is essential for growth of P. aeruginosa. WaaP was structurally similar to eukaryotic protein kinases and, intriguingly, was complexed with acylated-acyl carrier protein (acyl-ACP). WaaP produced by in vitro transcription-translation was insoluble unless acyl-ACP was present. WaaP variants designed to perturb the acyl-ACP interaction were less stable in cells and exhibited reduced kinase function. Mass spectrometry identified myristyl-ACP as the likely physiological binding partner for WaaP in P. aeruginosa. Together, these results demonstrate that acyl-ACP is required for WaaP protein solubility and kinase function. To the best of our knowledge, this is the first report describing acyl-ACP in the role of a cofactor necessary for the production and stability of a protein partner.

PubMed: 30237436
DOI: 10.1038/s41598-018-32379-1

実験手法

X-RAY DIFFRACTION (2.396 Å)