Department of Biochemistry, Molecular Biology and Biophysics, 6-155 Jackson Hall, 321 Church Street SE, University of Minnesota, MN 55455, USA.
J Mol Biol. 2011 May 6;408(3):379-98. doi: 10.1016/j.jmb.2011.02.047. Epub 2011 Feb 25.
Heme proteins are extremely diverse, widespread, and versatile biocatalysts, sensors, and molecular transporters. The chlorite dismutase family of hemoproteins received its name due to the ability of the first-isolated members to detoxify anthropogenic ClO(2)(-), a function believed to have evolved only in the last few decades. Family members have since been found in 15 bacterial and archaeal genera, suggesting ancient roots. A structure- and sequence-based examination of the family is presented, in which key sequence and structural motifs are identified, and possible functions for family proteins are proposed. Newly identified structural homologies moreover demonstrate clear connections to two other large, ancient, and functionally mysterious protein families. We propose calling them collectively the CDE superfamily of heme proteins.
血红素蛋白是一类非常多样、广泛和多功能的生物催化剂、传感器和分子转运蛋白。由于最初分离得到的成员具有解毒人为 ClO2(-)的能力，因此得名氯酸盐异构酶家族的血红素蛋白，这种功能被认为是在过去几十年中才进化出来的。此后，在 15 个细菌和古菌属中发现了该家族的成员，这表明其具有古老的起源。本文对该家族进行了基于结构和序列的研究，鉴定了关键的序列和结构模体，并提出了家族蛋白的可能功能。此外，新发现的结构同源性还表明与另外两个大型、古老且功能神秘的蛋白质家族存在明显联系。我们建议将它们统称为血红素蛋白的 CDE 超家族。
