5WSL

Structural studies of keratinase from Meiothermus taiwanensis WR-220

5WSL の概要

• エントリーDOI: 10.2210/pdb5wsl/pdb
• 分子名称: keratinase, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: keratainase, protease, hydrolase
• 由来する生物種: Meiothermus taiwanensis WR-220
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 93500.96

構造登録者

Ho, M.C.,Wu, S.H.,Chen, M.Y.,Tu, I.F. (登録日: 2016-12-07, 公開日: 2017-10-18, 最終更新日: 2024-10-23)

主引用文献

Wu, W.L.,Chen, M.Y.,Tu, I.F.,Lin, Y.C.,EswarKumar, N.,Chen, M.Y.,Ho, M.C.,Wu, S.H.
The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles
Sci Rep, 7:4658-4658, 2017

PubMed Abstract: Billions of tons of keratin bio-wastes are generated by poultry industry annually but discarded that result in serious environmental pollution. Keratinase is a broad spectrum protease with the unique ability to degrade keratin, providing an eco-friendly way to convert keratin wastes to valuable amino acids. In this report, a feather-degrading thermophilic bacterium, Meiothermus taiwanensis WR-220, was investigated due to its ability to apparently complete feather decay at 65 °C in two days. By genomics, proteomics, and biochemical approaches, the extracellular heat-stable keratinase (MtaKer) from M. taiwanensis WR-220 was identified. The recombinant MtaKer (rMtaKer) possesses keratinolytic activities at temperatures ranging from 25 to 75 °C and pH from 4 to 11, with a maximum keratinolytic activity at 65 °C and pH 10. The phylogenetic and structural analysis revealed that MtaKer shares low sequence identity but high structural similarity with known keratinases. Accordingly, our findings have enabled the discovery of more keratinases from other extremophiles, Thermus and Deinococcus. Proteins encoded in the extremophiles shall be evolved to be functional in the extreme conditions. Hence, our study expands the current boundary of hunting keratinases that can tolerate extreme conditions for keratin wastes biorecycle and other industrial applications.

PubMed: 28680127
DOI: 10.1038/s41598-017-04723-4

実験手法

X-RAY DIFFRACTION (1.5 Å)