9C19

Structure of human LIAS

9C19 の概要

• エントリーDOI: 10.2210/pdb9c19/pdb
• 分子名称: Lipoyl synthase, mitochondrial, Glycine cleavage system H protein, mitochondrial, IRON/SULFUR CLUSTER, ... (8 entities in total)
• 機能のキーワード: lipoyl synthase, lias, biosynthetic protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 185110.57

構造登録者

Esakova, O.A.,Warui, D.M.,Neti, S.S.,Alumasa, J.N.,Booker, S.J. (登録日: 2024-05-28, 公開日: 2025-07-09, 最終更新日: 2026-03-04)

主引用文献

Esakova, O.A.,Warui, D.M.,Neti, S.S.,Alumasa, J.N.,Booker, S.J.
Structural basis for catalysis by human lipoyl synthase.
Nat Commun, 16:6355-6355, 2025

PubMed Abstract: Lipoic acid is an essential cofactor in five mitochondrial multiprotein complexes. In each complex, it is tethered in an amide linkage to the side chain of a conserved lysyl residue on a lipoyl carrier protein or lipoyl domain to afford the lipoyl cofactor. Lipoyl synthase catalyzes the last step in the biosynthesis of the lipoyl cofactor, the addition of two sulfur atoms to carbons 6 and 8 of an octanoyllysyl residue of the H protein, the lipoyl carrier protein of the glycine cleavage system. Lipoyl synthase, a member of the radical S-adenosylmethionine superfamily, contains two [FeS] clusters, one of which is sacrificed during catalysis to supply the appended sulfur atoms. Herein, we use X-ray crystallography to characterize several stages in lipoyl synthase catalysis and present a structure of an intermediate wherein the enzyme is cross-linked to the H protein substrate through a 6-mercaptooctanoyl ligand to a [FeS] cluster.

PubMed: 40640146
DOI: 10.1038/s41467-025-61393-x

実験手法

X-RAY DIFFRACTION (2.58 Å)