一种O-连接的N-乙酰葡糖胺转移酶同源物的结构为深入了解细胞内糖基化提供了线索。
Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.
作者信息
Martinez-Fleites Carlos, Macauley Matthew S, He Yuan, Shen David L, Vocadlo David J, Davies Gideon J
机构信息
Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5YW, UK.
出版信息
Nat Struct Mol Biol. 2008 Jul;15(7):764-5. doi: 10.1038/nsmb.1443. Epub 2008 Jun 8.
N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site.
蛋白质的N-乙酰葡糖胺（O-GlcNAc）修饰通过与磷酸化的动态相互作用提供了一种控制多种细胞过程的机制。UDP-葡糖胺：多肽基转移酶（OGT）催化O-GlcNAc的添加。完整OGT同源物的结构及人OGT变体的动力学分析揭示了一条连续的超螺旋凹槽，该凹槽将底物导向活性位点。
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