5a35 | pdb_00005a35

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

spinqualitylabelsall models 5a35, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a35 is a 1 chain structure with sequence from Streptococcus pyogenes str. Manfredo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: 1PE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1JGN4_STRPD Publication Abstract from PubMed 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. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.,Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, Peleg AY, Leys D, Traven A, Ahel I Mol Cell. 2015 Jul 16;59(2):309-20. doi: 10.1016/j.molcel.2015.06.013. Epub 2015 , Jul 9. PMID:26166706 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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