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一种假定的原核生物电压门控Ca(2+)通道,每个亚基仅有一个6TM基序。

A putative prokaryote voltage-gated Ca(2+) channel with only one 6TM motif per subunit.

作者信息

Durell S R, Guy H R

机构信息

Molecular Structure Section, Laboratory of Experimental and Computational Biology, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, Maryland, 20892, USA.

出版信息

Biochem Biophys Res Commun. 2001 Mar 2;281(3):741-6. doi: 10.1006/bbrc.2001.4408.

Abstract

Until now, voltage-gated Ca(2+) channel proteins have been found only in eukaryotes. Here we report that a gene recently discovered in the eubacterium Bacillus halodurans codes for a protein closely related to eukaryotic Ca(2+) channels, but that has only one 6-transmembrane-segement (6TM) motif, instead of four, in its pore-forming subunit. This is supported by the comparison of consensus sequences, which, along with the patterns of residue conservation, indicates a similar structure in the membrane to voltage-gated K(+) channels. From this we hypothesize that Ca(2+) channels originally evolved in bacteria, and that the specific eubacteria protein highlighted here is an ideal candidate for structure determination efforts.

摘要

到目前为止,电压门控Ca(2+)通道蛋白仅在真核生物中被发现。在此我们报告,最近在真细菌嗜碱芽孢杆菌中发现的一个基因编码一种与真核Ca(2+)通道密切相关的蛋白质,但该蛋白质在其形成孔道的亚基中只有一个6跨膜片段(6TM)基序,而非四个。共有序列的比较支持了这一点,该比较连同残基保守模式表明其在膜中的结构与电压门控K(+)通道相似。据此我们推测Ca(2+)通道最初在细菌中进化,此处所强调的特定真细菌蛋白是结构测定研究的理想候选对象。

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