3RIG: Sirt5 is an NAD-dependent protein lysine demalonylase and desuccinylase

Citation:
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.
PDB ID: 3RIGDownload
MMDB ID: 95217
PDB Deposition Date: 2011/4/13
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 3RIG: dimeric; determined by author and by software (PISA)
Molecular Components in 3RIG
Label Count Molecule
Proteins (2 molecules)
1
Nad-dependent Deacetylase Sirtuin-5(Gene symbol: SIRT5)
Molecule annotation
1
Peptide of Histone 3 Thioacetyl-lysine 9
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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