4.5 Article

Structure, function and biogenesis of the fungal proton pump Pma1

出版社

ELSEVIER
DOI: 10.1016/j.bbamcr.2023.119600

关键词

Plasma membrane proton ATPase; Proton pump; Auto-inhibition; Structure-function relationship; Mutational data

向作者/读者索取更多资源

This article reviews the current progress in the study of the structure, function, and biogenesis of fungal Pma1 and introduces the recently determined high-resolution structures of Pma1 using cryo-electron microscopy, providing new insights into its stability, regulated activity, and druggability.
The fungal plasma membrane proton pump Pma1 is an integral plasma membrane protein of the P-type ATPase family. It is an essential enzyme responsible for maintaining a constant cytosolic pH and for energising the plasma membrane to secondary transport processes. Due to its importance for fungal survival and absence from animals, Pma1 is also a highly sought-after drug target. Until recently, its characterisation has been limited to functional, mutational and localisation studies, due to a lack of high-resolution structural information. The determination of three cryo-EM structures of Pma1 in its unique hexameric state offers a new level of understanding the molecular mechanisms underlying the protein's stability, regulated activity and druggability. In light of this context, this article aims to review what we currently know about the structure, function and biogenesis of fungal Pma1.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据