8Z54

Crystal structure of human SIRT5 in complex with succinylated Prx1 fragment

8Z54 の概要

• エントリーDOI: 10.2210/pdb8z54/pdb
• 分子名称: NAD-dependent protein deacylase sirtuin-5, mitochondrial, Peroxiredoxin-1 fragment, ZINC ION, ... (5 entities in total)
• 機能のキーワード: sirt5, succinyl lysine, deacylase, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31482.23

構造登録者

Yokoyama, T.,Takayama, Y. (登録日: 2024-04-18, 公開日: 2024-10-09)

主引用文献

Yokoyama, T.,Takayama, Y.,Mizuguchi, M.,Nabeshima, Y.,Kusaka, K.
SIRT5 mutants reveal the role of conserved asparagine and glutamine residues in the NAD + -binding pocket.
Febs Lett., 598:2269-2280, 2024

PubMed Abstract: SIRT5, one of the mammalian sirtuins, specifically recognizes succinyl-lysine residues on proteins and catalyzes the desuccinylation reaction. In this study, we characterized SIRT5 mutants with hydrophobic amino acid substitutions at Q140 and N141, in addition to the catalytic residue H158, known as an active site residue, by the Michaelis-Menten analysis and X-ray crystallography. Kinetic analysis showed that the catalytic efficiency (k/K) of the Q140L and N141V mutants decreased to 0.02 times and 0.0038 times that of the wild-type SIRT5, respectively, with the activity of the N141V mutant becoming comparable to that of the H158M mutant. Our findings indicate that N141 contributes significantly to the desuccinylation reaction.

PubMed: 39031546
DOI: 10.1002/1873-3468.14961

実験手法

X-RAY DIFFRACTION (1.45 Å)