5A35

Crystal structure of Glycine Cleavage Protein H-Like (GcvH-L) from Streptococcus pyogenes

5A35 の概要

• エントリーDOI: 10.2210/pdb5a35/pdb
• 関連するPDBエントリー: 5A3A 5A3B 5A3C
• 分子名称: GLYCINE CLEAVAGE SYSTEM H PROTEIN, PENTAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: transport protein, lipoylation, adp-ribosylation
• 由来する生物種: STREPTOCOCCUS PYOGENES
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13501.96

構造登録者

Rack, J.G.M.,Morra, R.,Barkauskaite, E.,Kraehenbuehl, R.,Ariza, A.,Qu, Y.,Ortmayer, M.,Leidecker, O.,Cameron, D.R.,Matic, I.,Peleg, A.Y.,Leys, D.,Traven, A.,Ahel, I. (登録日: 2015-05-27, 公開日: 2015-07-29, 最終更新日: 2024-01-10)

主引用文献

Rack, J.G.,Morra, R.,Barkauskaite, E.,Kraehenbuehl, R.,Ariza, A.,Qu, Y.,Ortmayer, M.,Leidecker, O.,Cameron, D.R.,Matic, I.,Peleg, A.Y.,Leys, D.,Traven, A.,Ahel, I.
Identification of a Class of Protein Adp-Ribosylating Sirtuins in Microbial Pathogens.
Mol.Cell, 59:309-, 2015

PubMed Abstract: Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activity. In our model organisms, Staphylococcus aureus and Streptococcus pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by a sirtuin-associated macrodomain protein. Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between lipoylation and mono-ADP-ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species.

PubMed: 26166706
DOI: 10.1016/J.MOLCEL.2015.06.013

実験手法

X-RAY DIFFRACTION (1.5 Å)