Chlorite Dismutases, DyPs, and EfeB: 3 Microbial Heme Enzyme Families Comprise the CDE Structural Superfamily

JOURNAL OF MOLECULAR BIOLOGY

卷:408

Article

Goblirsch, Brandon²  Kurker, Richard C.¹  Streit, Bennett R.¹  Wilmot, Carrie M.²  DuBois, Jennifer L.¹ 

[1] Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA

[2] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA

关键词: heme;    protein;    bacteria;    peroxidase;    oxygen;   

DOI  :  10.1016/j.jmb.2011.02.047

来源: Elsevier

【 摘 要 】

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 ClO2-, 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. (c) 2011 Elsevier Ltd. All rights reserved.

【 授权许可】

Free