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Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 A resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme

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Title
Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 A resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme
Other Titles
호냉성 박테리아 (Pseudoalteromonas arctica PAMC 21717) 유래 저온활성 단백질 분해효소 (Pro21717) 의 삼차구조연구
세재용 분해효소로써의 가능성 검증
Authors
Park, Ha Ju
Yim, Joung Han
Lee, Jun Hyuck
Bon-Hun Koo
Kim, Jung Eun
Han, Se Jong
Hackwon Do
Kim, Dockyu
Lee, Chang Woo
Keywords
Pro21717; Pseudoalteromonas arctica PAMC 21717; X-ray crystallography; crystal structure; serine protease
Issue Date
2018
Citation
Park, Ha Ju, et al. 2018. "Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 A resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme". PLOS ONE, 13: 1-20.
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 A. 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.
URI
http://repository.kopri.re.kr/handle/201206/6469
DOI
http://dx.doi.org/10.1371/journal.pone.0191740
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