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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystallization of a mammalian membrane protein overexpressed in Saccharomyces cerevisiae
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Crystallization of a mammalian membrane protein overexpressed in Saccharomyces cerevisiae

机译：在酿酒酵母中过表达的哺乳动物膜蛋白的结晶

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摘要

The Ca2+-ATPase SERCA1a (sarcoplasmic-endoplasmic reticulum Ca2+-ATPase isoform 1a) from rabbit has been overexpressed in Saccharomyces cerevisiae. This membrane protein was purified by avidin agarose affinity chromatography based on natural biotinylation in the expression host, followed by HPLC gel filtration. Both the functional and structural properties of the overexpressed protein validate the method. Thus, calcium-dependent ATPase activity and calcium transport are essentially intact after reconstitution in proteoliposomes. Moreover, the recombinant protein crystallizes in a form that is isomorphous to the native SERCA1a protein from rabbit, and the diffraction properties are similar. This represents a successful crystallization of a mammalian membrane protein derived from a heterologous expression system, and it opens the way for the study of mutant forms of SERCA1a.
机译：在酿酒酵母中，来自兔的Ca2 + -ATPase SERCA1a（肌浆-内质​​网Ca2 + -ATPase亚型1a）已过表达。通过基于表达宿主中天然生物素化的亲和素琼脂糖亲和色谱法纯化该膜蛋白，然后进行HPLC凝胶过滤。过表达蛋白质的功能和结构特性均验证了该方法。因此，在蛋白脂质体中重构后，钙依赖性ATP酶活性和钙转运基本上是完整的。而且，重组蛋白以与来自兔的天然SERCA1a蛋白同形的形式结晶，并且衍射特性相似。这代表了衍生自异源表达系统的哺乳动物膜蛋白的成功结晶，为研究SERCA1a的突变形式开辟了道路。

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