Membrane Protein Production in the Yeast P. pastoris.
Membrane Protein Production in the Yeast P. pastoris.
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毕赤酵母中的膜蛋白生产。
DOI：
10.1007/978-1-0716-2368-8_10
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发表时间：
2022
期刊：
影响因子：
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通讯作者：
Ayub H
中科院分区：
文献类型：
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作者：
Ayub H
重组哺乳动物膜蛋白的第一个晶体结构是使用在酵母细胞中产生的高质量蛋白质来解决的。其中之一，大鼠Kv1.2电压门控钾通道，在毕赤酵母中合成。从那时起，这种酵母物种一直是合成真核细胞膜蛋白的宿主的流行选择，因为它快速，容易，培养便宜，并且能够进行翻译后修饰。重组膜蛋白的最新结构。pastoris包括一系列人维生素K环氧化物还原酶的X射线晶体学结构和来自河豚的TMEM206质子激活氯离子通道的冷冻电子显微镜结构。巴斯德毕赤酵母也被用于结构和功能上表征一系列膜蛋白，包括四跨膜蛋白、水通道蛋白和G蛋白偶联受体。本章概述了这些成功的基础方法。
The first crystal structures of recombinant mammalian membrane proteins were solved using high-quality protein that had been produced in yeast cells. One of these, the rat Kv1.2 voltage-gated potassium channel, was synthesized inPichia pastoris. Since then, this yeast species has remained a consistently popular choice of host for synthesizing eukaryotic membrane proteins because it is quick, easy, and cheap to culture and is capable of posttranslational modification. Very recent structures of recombinant membrane proteins produced inP. pastorisinclude a series of X-ray crystallography structures of the human vitamin K epoxide reductase and a cryo-electron microscopy structure of the TMEM206 proton-activated chloride channel from pufferfish. P. pastorishas also been used to structurally and functionally characterize a range of membrane proteins including tetraspanins, aquaporins, and G protein-coupled receptors. This chapter provides an overview of the methodological approaches underpinning these successes.