Koehler Carla M
Department of Chemistry and Biochemistry and Molecular Biology Institute, UCLA, Los Angeles, CA 90095, USA.
Trends Biochem Sci. 2004 Jan;29(1):1-4. doi: 10.1016/j.tibs.2003.11.003.
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.
线粒体外膜间隙含有“小”Tim(内膜转位酶)蛋白,其特征是具有保守的“双Cx(3)C”基序,中间间隔11 - 16个残基。小Tim蛋白与内膜上的Tim22复合物一起,形成TIM22导入机制,介导多跨膜内膜蛋白的生物合成。初步研究时,保守基序类似于锌指样结构域,但半胱氨酸残基之间的间距与典型锌指不同。最近的出版物对保守半胱氨酸的功能提出了不同观点:半胱氨酸形成锌指样结构以配位锌,或者它们形成并列的二硫键。