4FQD

Crystal structure of the enolpyruvyl transferase NikO from Streptomyces tendae

4FQD の概要

• エントリーDOI: 10.2210/pdb4fqd/pdb
• 分子名称: NikO protein, SULFATE ION (3 entities in total)
• 機能のキーワード: beta/alpha inverse barrel, enolpyruvyl transferase, fosfomycin binding, transferase
• 由来する生物種: Streptomyces tendae
• 細胞内の位置: Cytoplasm (By similarity): Q712I1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103150.87

構造登録者

Oberdorfer, G.,Gruber, K. (登録日: 2012-06-25, 公開日: 2012-07-25, 最終更新日: 2023-09-13)

主引用文献

Oberdorfer, G.,Binter, A.,Ginj, C.,Macheroux, P.,Gruber, K.
Structural and functional characterization of NikO, an enolpyruvyl transferase essential in nikkomycin biosynthesis.
J.Biol.Chem., 287:31427-31436, 2012

PubMed Abstract: Nikkomycins are peptide-nucleoside compounds with fungicidal, acaricidal, and insecticidal properties because of their strong inhibition of chitin synthase. Thus, they are potential antibiotics especially for the treatment of immunosuppressed patients, for those undergoing chemotherapy, or after organ transplants. Although their chemical structure has been known for more than 30 years, only little is known about their complex biosynthesis. The genes encoding for proteins involved in the biosynthesis of the nucleoside moiety of nikkomycins are co-transcribed in the same operon, comprising the genes nikIJKLMNO. The gene product NikO was shown to belong to the family of enolpyruvyl transferases and to catalyze the transfer of an enolpyruvyl moiety from phosphoenolpyruvate to the 3'-hydroxyl group of UMP. Here, we report activity and inhibition studies of the wild-type enzyme and the variants C130A and D342A. The x-ray crystal structure revealed differences between NikO and its homologs. Furthermore, our studies led to conclusions concerning substrate binding and preference as well as to conclusions about inhibition/alkylation by the antibiotic fosfomycin.

PubMed: 22810238
DOI: 10.1074/jbc.M112.352096

実験手法

X-RAY DIFFRACTION (2.5 Å)