5e3b

Structure of macrodomain protein from Streptomyces coelicolor

spinqualitylabelsall models 5e3b, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e3b is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: EDO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9X7P1_STRCO Publication Abstract from PubMed ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and 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 synthesise 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 uncharacterised subfamily of macrodomain proteins. Its crystal structure revealed a highly conserved macrodomain fold. We showed that SCO6735 possesses the ability to hydrolyse 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. Disruption of macrodomain protein SCO6735 increases antibiotic production in Streptomyces coelicolor.,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 J Biol Chem. 2016 Sep 15. pii: jbc.M116.721894. PMID:27634042 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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