2E33
Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase
2E33 の概要
エントリーDOI | 10.2210/pdb2e33/pdb |
関連するPDBエントリー | 2E31 2E32 |
分子名称 | F-box only protein 2, Ribonuclease pancreatic, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
機能のキーワード | ubiquitin, scf, fbs1, rnaseb, ligase-hydrolase complex, ligase/hydrolase |
由来する生物種 | Mus musculus (house mouse) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 37212.78 |
構造登録者 | Mizushima, T.,Yoshida, Y.,Kumanomidou, T.,Hasegawa, Y.,Yamane, T.,Tanaka, K. (登録日: 2006-11-20, 公開日: 2007-03-20, 最終更新日: 2024-11-20) |
主引用文献 | Mizushima, T.,Yoshida, Y.,Kumanomidou, T.,Hasegawa, Y.,Suzuki, A.,Yamane, T.,Tanaka, K. Structural basis for the selection of glycosylated substrates by SCFFbs1 ubiquitin ligase Proc.Natl.Acad.Sci.Usa, 104:5777-5781, 2007 Cited by PubMed Abstract: The ubiquitin ligase complex SCF(Fbs1), which contributes to the ubiquitination of glycoproteins, is involved in the endoplasmic reticulum-associated degradation pathway. In SCF ubiquitin ligases, a diverse array of F-box proteins confers substrate specificity. Fbs1/Fbx2, a member of the F-box protein family, recognizes high-mannose oligosaccharides. To elucidate the structural basis of SCF(Fbs1) function, we determined the crystal structures of the Skp1-Fbs1 complex and the sugar-binding domain (SBD) of the Fbs1-glycoprotein complex. The mechanistic model indicated by the structures appears to be well conserved among the SCF ubiquitin ligases. The structure of the SBD-glycoprotein complex indicates that the SBD primarily recognizes Man(3)GlcNAc(2), thereby explaining the broad activity of the enzyme against various glycoproteins. Comparison of two crystal structures of the Skp1-Fbs1 complex revealed the relative motion of a linker segment between the F-box and the SBD domains, which might underlie the ability of the complex to recognize different acceptor lysine residues for ubiquitination. PubMed: 17389369DOI: 10.1073/pnas.0610312104 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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