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PDBsum entry 3wso
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References listed in PDB file
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Key reference
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Title
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The structural differences between a glycoprotein specific f-Box protein fbs1 and its homologous protein fbg3.
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Authors
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T.Kumanomidou,
K.Nishio,
K.Takagi,
T.Nakagawa,
A.Suzuki,
T.Yamane,
F.Tokunaga,
K.Iwai,
A.Murakami,
Y.Yoshida,
K.Tanaka,
T.Mizushima.
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Ref.
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Plos One, 2015,
10,
e0140366.
[DOI no: ]
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PubMed id
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Abstract
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The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in
diverse cellular processes and is one of the best-characterized ubiquitin
ligases. F-box proteins determine the substrate specificities of SCF ubiquitin
ligases. Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27
recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no
sugar-binding activity, despite the high sequence homology and conservation of
the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3. Here
we determined the crystal structure of the Skp1-FBG3 complex at a resolution of
2.6 Å. The substrate-binding domain of FBG3 is composed of a 10-stranded
antiparallel β-sandwich with three helices. Although the overall structure of
FBG3 is similar to that of Fbs1, the residues that form the Fbs1
carbohydrate-binding pocket failed to be superposed with the corresponding
residues of FBG3. Structure-based mutational analysis shows that distinct
hydrogen bond networks of four FBG3 loops, i.e., β2-β3, β5-β6, β7-β8, and
β9-β10, prevent the formation of the carbohydrate-binding pocket shown in Fbs1.
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