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• W4310700279 abstract "Abstract Arabidopsis glycosyltransferase family 41 (GT41) protein SPINDLY (SPY) plays pleiotropic roles in plant development. Despite the amino acid sequence is similar to human O-GlcNAc transferase, Arabidopsis SPY has been identified as a novel nucleocytoplasmic protein O-fucosyltransferase. SPY-like proteins extensively exist in diverse organisms, indicating that O-fucosylation by SPY is a common way to regulate intracellular protein functions. However, the details of how SPY recognizes and glycosylates substrates are unknown. Here, we present a crystal structure of Arabidopsis SPY/GDP complex at 2.85 Å resolution. SPY adopts a head-to-tail dimer. Strikingly, the conformation of a ‘catalytic SPY’/GDP/‘substrate SPY’ complex formed by two symmetry-related SPY dimers is captured in the crystal lattice. The structure together with mutagenesis and enzymatic data demonstrate SPY can fucosylate itself and SPY’s self-fucosylation region negatively regulates its enzyme activity, reveal SPY’s substrate recognition and enzyme mechanism, and provide insights into the glycan donor substrate selection in GT41 proteins." @default.
• W4310700279 created "2022-12-16" @default.
• W4310700279 creator A5007422464 @default.
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• W4310700279 date "2022-12-02" @default.
• W4310700279 modified "2023-10-05" @default.
• W4310700279 title "Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY" @default.
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• W4310700279 doi "https://doi.org/10.1038/s41467-022-35234-0" @default.
• W4310700279 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36456586" @default.
• W4310700279 hasPublicationYear "2022" @default.
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