5WLW
Crystal Structure of the Human Mitochondrial Cysteine Desulfurase with active Cysteine Loop within ISCU1 active site, coordinating Zn ion. Complexed with human ISD11 and E. coli ACP1 at 3.3A.
Summary for 5WLW
| Entry DOI | 10.2210/pdb5wlw/pdb |
| Related | 5WGB 5WKP |
| Descriptor | Cysteine desulfurase, mitochondrial, LYR motif-containing protein 4, Acyl carrier protein, ... (7 entities in total) |
| Functional Keywords | human mitochondrial cysteine desulfurse lyr motif containing protein 4 iron-sulfur cluster scaffold protein iscu1 with zn in the active site acyl carrier protein 1 (e.coli), transferase |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic: Cytoplasm: Q9Y697 Mitochondrion: Q9HD34 Cytoplasm : B7MJ81 Isoform 1: Mitochondrion . Isoform 2: Cytoplasm: Q9H1K1 |
| Total number of polymer chains | 8 |
| Total formula weight | 163100.69 |
| Authors | Boniecki, M.T.,Cygler, M. (deposition date: 2017-07-27, release date: 2017-11-15, Last modification date: 2023-10-04) |
| Primary citation | Boniecki, M.T.,Freibert, S.A.,Muhlenhoff, U.,Lill, R.,Cygler, M. Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex. Nat Commun, 8:1287-1287, 2017 Cited by PubMed Abstract: Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular functions including DNA maintenance, protein translation, and energy conversion. De novo Fe/S cluster synthesis occurs on the mitochondrial scaffold protein ISCU and requires cysteine desulfurase NFS1, ferredoxin, frataxin, and the small factors ISD11 and ACP (acyl carrier protein). Both the mechanism of Fe/S cluster synthesis and function of ISD11-ACP are poorly understood. Here, we present crystal structures of three different NFS1-ISD11-ACP complexes with and without ISCU, and we use SAXS analyses to define the 3D architecture of the complete mitochondrial Fe/S cluster biosynthetic complex. Our structural and biochemical studies provide mechanistic insights into Fe/S cluster synthesis at the catalytic center defined by the active-site Cys of NFS1 and conserved Cys, Asp, and His residues of ISCU. We assign specific regulatory rather than catalytic roles to ISD11-ACP that link Fe/S cluster synthesis with mitochondrial lipid synthesis and cellular energy status. PubMed: 29097656DOI: 10.1038/s41467-017-01497-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.317 Å) |
Structure validation
Download full validation report
