7DF2

Crystal structure of a C2 domain protein from Ramazzottius varieornatus

7DF2 の概要

• エントリーDOI: 10.2210/pdb7df2/pdb
• 分子名称: C2 domain protein, beta-D-glucopyranose-(1-1)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: tardigrade, ca-binding protein, c2 domain, metal binding protein
• 由来する生物種: Ramazzottius varieornatus (Water bear)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24342.22

構造登録者

Fukuda, Y.,Inoue, T. (登録日: 2020-11-06, 公開日: 2020-12-09, 最終更新日: 2024-10-23)

主引用文献

Fukuda, Y.,Inoue, T.
Structural insights into a C2 domain protein specifically found in tardigrades.
Protein Sci., 30:513-518, 2021

PubMed 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 Ca -binding sites, and hydrophobic residues on Ca -binding (CBD) loops, which resemble characteristics of C2 domain proteins. We therefore conveniently describe this protein as tardigrade C2 domain protein (TC2P). Because the C2 domain functions as a Ca -mediated membrane docking module, which is related to signal transduction or membrane trafficking, TC2Ps may play a role in Ca -triggered phenomenon under desiccated situations. Our finding provides not only structural insights into a newly discovered desiccation-related protein family but also insights into the evolution and diversity of C2 domain proteins.

PubMed: 33226149
DOI: 10.1002/pro.4002

実験手法

X-RAY DIFFRACTION (1.7 Å)