5E3B

Structure of macrodomain protein from Streptomyces coelicolor

5E3B の概要

• エントリーDOI: 10.2210/pdb5e3b/pdb
• 分子名称: Macrodomain protein, SODIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: macrodomain protein, hydrolase
• 由来する生物種: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19673.23

構造登録者

Lalic, J.,Posavec Marjanovic, M.,Perina, D.,Sabljic, I.,Zaja, R.,Plese, B.,Imesek, M.,Bucca, G.,Ahel, M.,Cetkovic, H.,Luic, M.,Mikoc, A.,Ahel, I. (登録日: 2015-10-02, 公開日: 2016-09-28, 最終更新日: 2024-01-10)

主引用文献

Lalic, J.,Posavec Marjanovic, M.,Palazzo, L.,Perina, D.,Sabljic, I.,Zaja, R.,Colby, T.,Plese, B.,Halasz, M.,Jankevicius, G.,Bucca, G.,Ahel, M.,Matic, I.,Cetkovic, H.,Luic, M.,Mikoc, A.,Ahel, I.
Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor.
J.Biol.Chem., 291:23175-23187, 2016

PubMed Abstract: ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and that controls many important cellular processes. Macrodomains are evolutionarily conserved structural domains that bind ADP-ribose derivatives and are found in proteins with diverse cellular functions. Some proteins from the macrodomain family can hydrolyze ADP-ribosylated substrates and therefore reverse this post-translational modification. Bacteria and Streptomyces, in particular, are known to utilize protein ADP-ribosylation, yet very little is known about their enzymes that synthesize and remove this modification. We have determined the crystal structure and characterized, both biochemically and functionally, the macrodomain protein SCO6735 from Streptomyces coelicolor This protein is a member of an uncharacterized subfamily of macrodomain proteins. Its crystal structure revealed a highly conserved macrodomain fold. We showed that SCO6735 possesses the ability to hydrolyze PARP-dependent protein ADP-ribosylation. Furthermore, we showed that expression of this protein is induced upon DNA damage and that deletion of this protein in S. coelicolor increases antibiotic production. Our results provide the first insights into the molecular basis of its action and impact on Streptomyces metabolism.

PubMed: 27634042
DOI: 10.1074/jbc.M116.721894

実験手法

X-RAY DIFFRACTION (1.6 Å)