3OER
Crystal structure of trimeric frataxin from the yeast saccharomyces cerevisiae, complexed with cobalt
3OER の概要
エントリーDOI | 10.2210/pdb3oer/pdb |
関連するPDBエントリー | 2FQL 3OEQ |
分子名称 | Frataxin homolog, mitochondrial, COBALT (II) ION (3 entities in total) |
機能のキーワード | alpha/beta sandwich, metallochaperone, iron-storage, transport protein |
由来する生物種 | Saccharomyces cerevisiae (yeast) |
細胞内の位置 | Mitochondrion matrix : Q07540 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 13730.12 |
構造登録者 | Soderberg, C.A.G.,Rajan, S.,Gakh, O.,Ta, C.,Isaya, G.,Al-Karadaghi, S. (登録日: 2010-08-13, 公開日: 2011-08-24, 最終更新日: 2023-09-06) |
主引用文献 | Soderberg, C.A.,Shkumatov, A.V.,Rajan, S.,Gakh, O.,Svergun, D.I.,Isaya, G.,Al-Karadaghi, S. Oligomerization Propensity and Flexibility of Yeast Frataxin Studied by X-ray Crystallography and Small-Angle X-ray Scattering. J.Mol.Biol., 414:783-797, 2011 Cited by PubMed Abstract: Frataxin is a mitochondrial protein with a central role in iron homeostasis. Defects in frataxin function lead to Friedreich's ataxia, a progressive neurodegenerative disease with childhood onset. The function of frataxin has been shown to be closely associated with its ability to form oligomeric species; however, the factors controlling oligomerization and the types of oligomers present in solution are a matter of debate. Using small-angle X-ray scattering, we found that Co(2+), glycerol, and a single amino acid substitution at the N-terminus, Y73A, facilitate oligomerization of yeast frataxin, resulting in a dynamic equilibrium between monomers, dimers, trimers, hexamers, and higher-order oligomers. Using X-ray crystallography, we found that Co(2+) binds inside the channel at the 3-fold axis of the trimer, which suggests that the metal has an oligomer-stabilizing role. The results reveal the types of oligomers present in solution and support our earlier suggestions that the trimer is the main building block of yeast frataxin oligomers. They also indicate that different mechanisms may control oligomer stability and oligomerization in vivo. PubMed: 22051511DOI: 10.1016/j.jmb.2011.10.034 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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