3RIY
Sirt5 is an NAD-dependent protein lysine demalonylase and desuccinylase
Summary for 3RIY
| Entry DOI | 10.2210/pdb3riy/pdb |
| Related | 3RIG |
| Descriptor | NAD-dependent deacetylase sirtuin-5, peptide of histone 3 N-succinyl lysine 9, ZINC ION, ... (5 entities in total) |
| Functional Keywords | desuccinylase, demalonylase, posttranslational modification, zn-binding domain, rossmann fold domain, hydrolase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Mitochondrion matrix. Isoform 1: Cytoplasm . Isoform 2: Mitochondrion : Q9NXA8 |
| Total number of polymer chains | 4 |
| Total formula weight | 63478.23 |
| Authors | |
| Primary citation | 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 Cited by 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: 22076378DOI: 10.1126/science.1207861 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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