Secondary structure reshuffling modulates glycosyltransferase function at the membrane
Secondary structure reshuffling modulates glycosyltransferase function at the membrane
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DOI：
10.1038/nchembio.1694
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发表时间：
2015-01-01
影响因子：
14.8
通讯作者：
Alzari, Pedro M.
中科院分区：
文献类型：
--
作者：
Giganti, David;Albesa-Jove, David;Alzari, Pedro M.
二级结构重折叠是生物学中的一个关键事件，因为它调节细胞中许多蛋白质的构象，产生功能或异常状态。甘露糖转移酶PIMA的晶体结构揭示了该蛋白质在催化循环中具有特殊的灵活性，包括从β链到α螺旋和从α螺旋到β链的转变。这些结构变化调节催化，并通过蛋白质与膜上的阴离子磷脂的相互作用而促进。
Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including beta-strand-to-alpha-helix and alpha-helix-to-beta-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.