卷曲螺旋-螺旋-卷曲螺旋-螺旋蛋白可能是氧化还原蛋白。

The coiled coil-helix-coiled coil-helix proteins may be redox proteins.

作者信息

Banci Lucia, Bertini Ivano, Ciofi-Baffoni Simone, Tokatlidis Kostas

机构信息

Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

出版信息

FEBS Lett. 2009 Jun 5;583(11):1699-702. doi: 10.1016/j.febslet.2009.03.061. Epub 2009 Apr 2.

DOI:10.1016/j.febslet.2009.03.061

PMID:19345215

Abstract

A number of nuclear encoded proteins are imported in to the intermembrane space of mitochondria where they adopt a coiled coil-helix-coiled coil-helix (CHCH) fold. Two disulfide bonds formed by twin CX(3)C or CX(9)C motifs stabilize this fold. Some of these proteins are also characterized at their N-termini by the presence of two additional cysteine residues which can perform oxidoreductase or metallochaperone functions or both. This fold represents the most 'minimal' oxidoreductase domain described so far.

摘要

许多核编码蛋白被导入线粒体的膜间隙，在那里它们形成卷曲螺旋-螺旋-卷曲螺旋-螺旋（CHCH）折叠结构。由双CX(3)C或CX(9)C基序形成的两个二硫键稳定了这种折叠结构。其中一些蛋白在其N端还具有另外两个半胱氨酸残基，它们可以发挥氧化还原酶或金属伴侣功能，或两者兼而有之。这种折叠结构代表了迄今为止描述的最“最小化”的氧化还原酶结构域。