3RIY

Sirt5 is an NAD-dependent protein lysine demalonylase and desuccinylase

3RIY の概要

• エントリーDOI: 10.2210/pdb3riy/pdb
• 関連するPDBエントリー: 3RIG
• 分子名称: NAD-dependent deacetylase sirtuin-5, peptide of histone 3 N-succinyl lysine 9, ZINC ION, ... (5 entities in total)
• 機能のキーワード: desuccinylase, demalonylase, posttranslational modification, zn-binding domain, rossmann fold domain, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Mitochondrion matrix. Isoform 1: Cytoplasm . Isoform 2: Mitochondrion : Q9NXA8
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63478.23

構造登録者

Zhou, Y.,Hao, Q. (登録日: 2011-04-14, 公開日: 2011-11-23, 最終更新日: 2023-11-01)

主引用文献

Du, J.,Zhou, Y.,Su, X.,Yu, J.J.,Khan, S.,Jiang, H.,Kim, J.,Woo, J.,Kim, J.H.,Choi, B.H.,He, B.,Chen, W.,Zhang, S.,Cerione, R.A.,Auwerx, J.,Hao, Q.,Lin, H.
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
Science, 334:806-809, 2011

PubMed Abstract: Silent information regulator 2 (Sir2) proteins (sirtuins) are nicotinamide adenine dinucleotide-dependent deacetylases that regulate important biological processes. Mammals have seven sirtuins, Sirt1 to Sirt7. Four of them (Sirt4 to Sirt7) have no detectable or very weak deacetylase activity. We found that Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro. The preference for succinyl and malonyl groups was explained by the presence of an arginine residue (Arg(105)) and tyrosine residue (Tyr(102)) in the acyl pocket of Sirt5. Several mammalian proteins were identified with mass spectrometry to have succinyl or malonyl lysine modifications. Deletion of Sirt5 in mice appeared to increase the level of succinylation on carbamoyl phosphate synthase 1, which is a known target of Sirt5. Thus, protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo.

PubMed: 22076378
DOI: 10.1126/science.1207861

実験手法

X-RAY DIFFRACTION (1.55 Å)