8TSK
Structure of human LIAS in the presence of 5'-deoxyadenosine and octanoyl-modified peptide
Summary for 8TSK
| Entry DOI | 10.2210/pdb8tsk/pdb |
| Descriptor | Lipoyl synthase, mitochondrial, IRON/SULFUR CLUSTER, METHIONINE, ... (7 entities in total) |
| Functional Keywords | lipoyl synthase, lias, biosynthetic protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 85278.75 |
| Authors | Esakova, O.A.,Warui, D.M.,Neti, S.S.,Alumasa, J.N.,Booker, S.J. (deposition date: 2023-08-11, release date: 2025-06-11, Last modification date: 2026-03-04) |
| Primary citation | 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 Cited by 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: 40640146DOI: 10.1038/s41467-025-61393-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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