6GEU
Crystal structure of the C230A mutant of human IBA57
Summary for 6GEU
| Entry DOI | 10.2210/pdb6geu/pdb |
| Related | 5OLI 6ESR 6QE3 6QE4 |
| Descriptor | Putative transferase CAF17, mitochondrial (2 entities in total) |
| Functional Keywords | mitochondrial protein, fe-s protein biogenesis, infantile leukodystrophy, protein binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 33767.78 |
| Authors | Calderone, V.,Ciofi-Baffoni, S.,Gourdoupis, S.,Banci, L.,Nasta, V. (deposition date: 2018-04-27, release date: 2019-04-03, Last modification date: 2024-01-17) |
| Primary citation | Gourdoupis, S.,Nasta, V.,Calderone, V.,Ciofi-Baffoni, S.,Banci, L. IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex. J.Am.Chem.Soc., 140:14401-14412, 2018 Cited by PubMed Abstract: The maturation of mitochondrial iron-sulfur proteins requires a complex protein machinery. Human IBA57 protein was proposed to act in a late phase of this machinery, along with GLRX5, ISCA1, and ISCA2. However, a molecular picture on how these proteins cooperate is not defined yet. We show here that IBA57 forms a heterodimeric complex with ISCA2 by bridging a [2Fe-2S] cluster, that [2Fe-2S] cluster binding is absolutely required to promote the complex formation, and that the cysteine of the conserved motif characterizing IBA57 protein family and the three conserved cysteines of the ISCA protein family act as cluster ligands. The [2Fe-2S] heterodimeric complex is the final product when IBA57 is either exposed to [2Fe-2S] ISCA2 or in the presence of [2Fe-2S] GLRX5 and apo ISCA2. We also find that the [2Fe-2S] ISCA2-IBA57 complex is resistant to highly oxidative environments and is capable of reactivating apo aconitase in vitro. Collectively, our data delinate a [2Fe-2S] cluster transfer pathway involving three partner proteins of the mitochondrial ISC machinery, that is, GLRX5, ISCA2 and IBA57, which leads to the formation of a [2Fe-2S] ISCA2-IBA57 complex. PubMed: 30269484DOI: 10.1021/jacs.8b09061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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