A perspective on structural and mechanistic aspects of protein O-fucosylation.
A perspective on structural and mechanistic aspects of protein O-fucosylation.
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DOI：
10.1107/s2053230x18004788
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发表时间：
2018-08-01
期刊：
影响因子：
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通讯作者：
Hurtado-Guerrero R
中科院分区：
文献类型：
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作者：
Lira-Navarrete E;Hurtado-Guerrero R
蛋白O-岩藻糖基转移酶1和2执行相同的转录后修饰，尽管底物不同。底物的正确折叠对于蛋白质识别是至关重要的，这些蛋白质的晶体结构已经表明了这两种蛋白质高度特异的机制。蛋白质O-岩藻糖基化是一种重要的翻译后修饰(PTM)，存在于蛋白质中的富含半胱氨酸的重复序列中。蛋白O-岩藻糖基转移酶1和2(PoFUT1和PoFUT2)是负责这种PTM的酶，并选择性地糖基化表皮生长因子样重复序列(EGF)和凝血酶反应蛋白I型重复序列(TSRs)中的特定残基。在过去的六年里，这两种酶的晶体结构都得到了报道，揭示了它们如何识别蛋白质底物和实现催化的重要信息。在这里，总结了目前可用的结构信息，并讨论了PoFUT1和PoFUT2如何采用不同的催化机理。
Protein O-fucosyltransferases 1 and 2 perform the same post-transcriptional modification albeit on different substrates. Correct folding of the substrates is essential for protein recognition, and the crystal structures of these proteins have shown the mechanism of how these two proteins are highly specific. Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs), respectively. Within the past six years, crystal structures of both enzymes have been reported, revealing important information on how they recognize protein substrates and achieve catalysis. Here, the structural information available today is summarized and how PoFUT1 and PoFUT2 employ different catalytic mechanisms is discussed.