Structural insights into a C2 domain protein specifically found in tardigrades.

ABSTRACT: Some tardigrades can survive extremely desiccated conditions through transition into a state called anhydrobiosis. Anhydrobiotic tardigrades have proteins unique to them and they are thought to be keys to the understanding of unusual desiccation resistance. In fact, previous transcriptome data show that several tardigrade-specific proteins are significantly upregulated under desiccated conditions. However, their physiological roles and chemical properties have been ambiguous because they show low or no similarity of amino acid sequences to proteins found in other organisms. Here, we report a crystal structure of one of such proteins. This protein shows a β-sandwich structure composed of 8 β-strands, three Ca²⁺ -binding sites, and hydrophobic residues on Ca²⁺ -binding

SUBMITTER: Fukuda Y 

PROVIDER: S-EPMC7784755 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature