4QJL

Crystal structure of M. ulcerans phosphopantetheinyl transferase MuPPT

4QJL の概要

• エントリーDOI: 10.2210/pdb4qjl/pdb
• 関連するPDBエントリー: 4QJK
• 分子名称: Phosphopantetheinyl transferase, PptII, COENZYME A, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: phosphopantetheinyl transferase, coa binding, transferase
• 由来する生物種: Mycobacterium ulcerans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26530.24

構造登録者

Noel, J.P.,Burkart, M.D.,Vickery, C.R. (登録日: 2014-06-04, 公開日: 2014-07-16, 最終更新日: 2024-02-28)

主引用文献

Vickery, C.R.,Kosa, N.M.,Casavant, E.P.,Duan, S.,Noel, J.P.,Burkart, M.D.
Structure, biochemistry, and inhibition of essential 4'-phosphopantetheinyl transferases from two species of mycobacteria.
Acs Chem.Biol., 9:1939-1944, 2014

PubMed Abstract: 4'-Phosphopantetheinyl transferases (PPTase) post-translationally modify carrier proteins with a phosphopantetheine moiety, an essential reaction in all three domains of life. In the bacterial genus Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors. We solved the X-ray crystal structures and biochemically characterized the Sfp-type PPTases from two of the most prevalent Mycobacterial pathogens, PptT of M. tuberculosis and MuPPT of M. ulcerans. Structural analyses reveal significant differences in cofactor binding and active site composition when compared to previously characterized Sfp-type PPTases. Functional analyses including the efficacy of Sfp-type PPTase-specific inhibitors also suggest that the Mycobacterial Sfp-type PPTases can serve as therapeutic targets against Mycobacterial infections.

PubMed: 24963544
DOI: 10.1021/cb500263p

実験手法

X-RAY DIFFRACTION (1.65 Å)