2HES

Cytosolic Iron-sulphur Assembly Protein- 1

2HES の概要

• エントリーDOI: 10.2210/pdb2hes/pdb
• 分子名称: Ydr267cp, CALCIUM ION (3 entities in total)
• 機能のキーワード: beta-propeller, wd40 repeat, biosynthetic protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: Q05583
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37355.57

構造登録者

Srinivasan, V.,Michel, H.,Lill, R.,Daili, J.A.N.,Pierik, A.J. (登録日: 2006-06-22, 公開日: 2007-07-03, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)