2HES

Cytosolic Iron-sulphur Assembly Protein- 1

Summary for 2HES

• Entry DOI: 10.2210/pdb2hes/pdb
• Descriptor: Ydr267cp, CALCIUM ION (3 entities in total)
• Functional Keywords: beta-propeller, wd40 repeat, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: Q05583
• Total number of polymer chains: 1
• Total formula weight: 37355.57

Authors

Srinivasan, V.,Michel, H.,Lill, R.,Daili, J.A.N.,Pierik, A.J. (deposition date: 2006-06-22, release date: 2007-07-03, Last modification date: 2024-02-14)

Primary citation

Srinivasan, V.,Netz, D.J.,Webert, H.,Mascarenhas, J.,Pierik, A.J.,Michel, H.,Lill, R.
Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in Iron-Sulfur Protein Biogenesis.
Structure, 15:1246-1257, 2007

PubMed Abstract: The WD40-repeat protein Cia1 is an essential, conserved member of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery in eukaryotes. Here, we report the crystal structure of Saccharomyces cerevisiae Cia1 to 1.7 A resolution. The structure folds into a beta propeller with seven blades pseudo symmetrically arranged around a central axis. Structure-based sequence alignment of Cia1 proteins shows that the WD40 propeller core elements are highly conserved. Site-directed mutagenesis of amino acid residues in loop regions with high solvent accessibility identified that the conserved top surface residue R127 performs a critical function: the R127 mutant cells grew slowly and were impaired in cytosolic Fe/S protein assembly. Human Ciao1, which reportedly interacts with the Wilms' tumor suppressor, WT1, is structurally similar to yeast Cia1. We show that Ciao1 can functionally replace Cia1 and support cytosolic Fe/S protein biogenesis. Hence, our structural and biochemical studies indicate the conservation of Cia1 function in eukaryotes.

PubMed: 17937914
DOI: 10.1016/j.str.2007.08.009

Experimental method

X-RAY DIFFRACTION (1.7 Å)