The small tim proteins and the twin CX3C motif
The small tim proteins and the twin CX3C motif
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DOI：
10.1016/j.tibs.2003.11.003
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发表时间：
2004-01-01
影响因子：
13.8
通讯作者：
Koehler, CM
中科院分区：
文献类型：
--
作者：
Koehler, CM
线粒体膜间隙含有“小”Tim（内膜转位酶）蛋白，其由其保守的“双Cx（3）C”基序标记，所述双Cx（3）C“基序由11-16个残基分开。小Tim蛋白与内膜上的Tim 22复合物一起形成TIM 22输入机制，其介导多位内膜蛋白的生物发生。在第一次调查时，保守的模体类似于锌指样结构域，但半胱氨酸残基之间的间距不同于典型的锌指。最近的出版物提出了不同的观点保守的半胱氨酸的功能：半胱氨酸形成锌指状结构，以协调锌，或者，它们形成并列的二硫键。
The mitochondrial intermembrane space contains the 'small' Tim (translocase of inner membrane) proteins that are marked by their conserved 'twin Cx(3)C' Motif separated by 11-16 residues. Together with the Tim22 complex at the inner membrane, the small Tim proteins form the TIM22 import machinery that mediates the biogenesis of polytopic inner membrane proteins. Upon first investigation, the conserved motif resembles a zinc-finger-like domain, but the spacing between the cysteine residues differs from that a canonical zinc finger. Recent publications present different views about the function of the conserved cysteines: the cysteines form a zinc-finger-like structure to coordinate zinc or, alternatively, they form juxtapositioned disulfide bonds.