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3GLR

Crystal Structure of human SIRT3 with acetyl-lysine AceCS2 peptide

Summary for 3GLR
Entry DOI10.2210/pdb3glr/pdb
Related3GLS 3GLT 3GLU
DescriptorNAD-dependent deacetylase sirtuin-3, mitochondrial, Acetyl-coenzyme A synthetase 2-like, mitochondrial, ZINC ION, ... (7 entities in total)
Functional Keywordsnad dependent deacetylase, sirtuin, substrate peptide complex, hydrolase, metal-binding, mitochondrion, nad, transit peptide, ligase, hydrolase-hydrolase regulator complex, hydrolase/hydrolase regulator
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight33541.87
Authors
Jin, L.,Wei, W.,Jiang, Y.,Peng, H.,Cai, J.,Mao, C.,Dai, H.,Bemis, J.E.,Jirousek, M.R.,Milne, J.C.,Westphal, C.H.,Perni, R.B. (deposition date: 2009-03-12, release date: 2009-06-16, Last modification date: 2024-10-09)
Primary citationJin, L.,Wei, W.,Jiang, Y.,Peng, H.,Cai, J.,Mao, C.,Dai, H.,Choy, W.,Bemis, J.E.,Jirousek, M.R.,Milne, J.C.,Westphal, C.H.,Perni, R.B.
Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes.
J.Biol.Chem., 284:24394-24405, 2009
Cited by
PubMed Abstract: SIRT3 is a major mitochondrial NAD(+)-dependent protein deacetylase playing important roles in regulating mitochondrial metabolism and energy production and has been linked to the beneficial effects of exercise and caloric restriction. SIRT3 is emerging as a potential therapeutic target to treat metabolic and neurological diseases. We report the first sets of crystal structures of human SIRT3, an apo-structure with no substrate, a structure with a peptide containing acetyl lysine of its natural substrate acetyl-CoA synthetase 2, a reaction intermediate structure trapped by a thioacetyl peptide, and a structure with the dethioacetylated peptide bound. These structures provide insights into the conformational changes induced by the two substrates required for the reaction, the acetylated substrate peptide and NAD(+). In addition, the binding study by isothermal titration calorimetry suggests that the acetylated peptide is the first substrate to bind to SIRT3, before NAD(+). These structures and biophysical studies provide key insight into the structural and functional relationship of the SIRT3 deacetylation activity.
PubMed: 19535340
DOI: 10.1074/jbc.M109.014928
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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