Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY

Li Zhu, Xiting Wei, Jianming Cong, Jing Zou, Lihao Wan and Shutong Xu ()
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Li Zhu: Huazhong Agricultural University
Xiting Wei: Huazhong Agricultural University
Jianming Cong: Huazhong Agricultural University
Jing Zou: Huazhong Agricultural University
Lihao Wan: Huazhong Agricultural University
Shutong Xu: Huazhong Agricultural University

Nature Communications, 2022, vol. 13, issue 1, 1-13

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.

Date: 2022
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DOI: 10.1038/s41467-022-35234-0

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