5YL7

Proteases from Pseudoalteromonas arctica PAMC 21717 (Pro21717)

5YL7 の概要

• エントリーDOI: 10.2210/pdb5yl7/pdb
• 分子名称: Pseudoalteromonas arctica PAMC 21717, Copurified unknown peptide, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: serine protease, psychrophilic bacterium, pseudoalteromonas arctica, hydrolase
• 由来する生物種: Pseudoalteromonas arctica; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35257.05

構造登録者

Lee, J.H.,Lee, C.W. (登録日: 2017-10-17, 公開日: 2018-01-31, 最終更新日: 2024-11-06)

主引用文献

Park, H.J.,Lee, C.W.,Kim, D.,Do, H.,Han, S.J.,Kim, J.E.,Koo, B.H.,Lee, J.H.,Yim, J.H.
Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 angstrom resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme
PLoS ONE, 13:e0191740-e0191740, 2018

PubMed Abstract: Enzymes isolated from organisms found in cold habitats generally exhibit higher catalytic activity at low temperatures than their mesophilic homologs and are therefore known as cold-active enzymes. Cold-active proteases are very useful in a variety of biotechnological applications, particularly as active ingredients in laundry and dishwashing detergents, where they provide strong protein-degrading activity in cold water. We identified a cold-active protease (Pro21717) from a psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, and determined the crystal structure of its catalytic domain (CD) at a resolution of 1.4 Å. The Pro21717-CD structure shows a conserved subtilisin-like fold with a typical catalytic triad (Asp185, His244, and Ser425) and contains four calcium ions and three disulfide bonds. Interestingly, we observed an unexpected electron density at the substrate-binding site from a co-purified peptide. Although the sequence of this peptide is unknown, analysis of the peptide-complexed structure nonetheless provides some indication of the substrate recognition and binding mode of Pro21717. Moreover, various parameters, including a wide substrate pocket size, an abundant active-site loop content, and a flexible structure provide potential explanations for the cold-adapted properties of Pro21717. In conclusion, this is first structural characterization of a cold-adapted subtilisin-like protease, and these findings provide a structural and functional basis for industrial applications of Pro21717 as a cold-active laundry or dishwashing detergent enzyme.

PubMed: 29466378
DOI: 10.1371/journal.pone.0191740

実験手法

X-RAY DIFFRACTION (1.4 Å)