3U31

Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine

3U31 の概要

• エントリーDOI: 10.2210/pdb3u31/pdb
• 関連するPDBエントリー: 3U3D
• 分子名称: Transcriptional regulatory protein sir2 homologue, histone 3 myristoyl lysine 9 peptide, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: zn-binding domain, rossmann fold domain, nad-dependent deacylase, nuclear, hydrolase
• 由来する生物種: Plasmodium falciparum; 詳細
• 細胞内の位置: Nucleus, nucleolus: Q8IE47
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34489.09

構造登録者

Zhou, Y.,Hao, Q. (登録日: 2011-10-04, 公開日: 2011-11-09, 最終更新日: 2023-11-01)

主引用文献

Zhu, A.Y.,Zhou, Y.,Khan, S.,Deitsch, K.W.,Hao, Q.,Lin, H.
Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl Lysine
Acs Chem.Biol., 2011

PubMed Abstract: Plasmodium falciparum Sir2A (PfSir2A), a member of the sirtuin family of nicotinamide adenine dinucleotide-dependent deacetylases, has been shown to regulate the expression of surface antigens to evade the detection by host immune surveillance. It is thought that PfSir2A achieves this by deacetylating histones. However, the deacetylase activity of PfSir2A is weak. Here we present enzymology and structural evidence supporting that PfSir2A catalyzes the hydrolysis of medium and long chain fatty acyl groups from lysine residues more efficiently. Furthermore, P. falciparum proteins are found to contain such fatty acyl lysine modifications that can be removed by purified PfSir2A in vitro. Together, the data suggest that the physiological function of PfSir2A in antigen variation may be achieved by removing medium and long chain fatty acyl groups from protein lysine residues. The robust activity of PfSir2A would also facilitate the development of PfSir2A inhibitors, which may have therapeutic value in malaria treatment.

PubMed: 21992006
DOI: 10.1021/cb200230x

実験手法

X-RAY DIFFRACTION (2.2 Å)