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1umh
From Proteopedia
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'''Structural basis of sugar-recognizing ubiquitin ligase''' | '''Structural basis of sugar-recognizing ubiquitin ligase''' | ||
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[[Category: Yamaguchi, Y.]] | [[Category: Yamaguchi, Y.]] | ||
[[Category: Yoshida, Y.]] | [[Category: Yoshida, Y.]] | ||
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Scf]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Ubiquitin]] |
| - | [[Category: | + | [[Category: Ubiquitin ligase]] |
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Revision as of 08:25, 3 May 2008
Structural basis of sugar-recognizing ubiquitin ligase
Overview
SCF(Fbs1) is a ubiquitin ligase that functions in the endoplasmic reticulum (ER)-associated degradation pathway. Fbs1/Fbx2, a member of the F-box proteins, recognizes high-mannose oligosaccharides. Efficient binding to an N-glycan requires di-N-acetylchitobiose (chitobiose). Here we report the crystal structures of the sugar-binding domain (SBD) of Fbs1 alone and in complex with chitobiose. The SBD is composed of a ten-stranded antiparallel beta-sandwich. The structure of the SBD-chitobiose complex includes hydrogen bonds between Fbs1 and chitobiose and insertion of the methyl group of chitobiose into a small hydrophobic pocket of Fbs1. Moreover, NMR spectroscopy has demonstrated that the amino acid residues adjoining the chitobiose-binding site interact with the outer branches of the carbohydrate moiety. Considering that the innermost chitobiose moieties in N-glycans are usually involved in intramolecular interactions with the polypeptide moieties, we propose that Fbs1 interacts with the chitobiose in unfolded N-glycoprotein, pointing the protein moiety toward E2 for ubiquitination.
About this Structure
1UMH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of sugar-recognizing ubiquitin ligase., Mizushima T, Hirao T, Yoshida Y, Lee SJ, Chiba T, Iwai K, Yamaguchi Y, Kato K, Tsukihara T, Tanaka K, Nat Struct Mol Biol. 2004 Apr;11(4):365-70. Epub 2004 Feb 29. PMID:14990996 Page seeded by OCA on Sat May 3 11:25:37 2008
Categories: Mus musculus | Single protein | Ubiquitin--protein ligase | Chiba, T. | Hirao, T. | Iwai, K. | Kato, K. | Lee, S J. | Mizushima, T. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Tanaka, K. | Tsukihara, T. | Yamaguchi, Y. | Yoshida, Y. | Lectin | Riken structural genomics/proteomics initiative | Rsgi | Scf | Structural genomic | Ubiquitin | Ubiquitin ligase
