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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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Cited 1 time in scopus
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dc.contributor.authorPark, Ha Ju-
dc.contributor.authorYim, Joung Han-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorBon-Hun Koo-
dc.contributor.authorKim, Jung Eun-
dc.contributor.authorHan, Se Jong-
dc.contributor.authorHackwon Do-
dc.contributor.authorKim, Dockyu-
dc.contributor.authorLee, Chang Woo-
dc.date.accessioned2018-03-20T13:56:24Z-
dc.date.available2018-03-20T13:56:24Z-
dc.date.issued2018-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/6469-
dc.description.abstractEnzymes 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.-
dc.languageEnglish-
dc.subject.classificationKing Sejong Station-
dc.titleCrystal 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-
dc.title.alternative호냉성 박테리아 (Pseudoalteromonas arctica PAMC 21717) 유래 저온활성 단백질 분해효소 (Pro21717) 의 삼차구조연구-
dc.title.alternative세재용 분해효소로써의 가능성 검증-
dc.typeArticle-
dc.identifier.bibliographicCitationPark, 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". <em>PLOS ONE</em>, 13: 1-20.-
dc.citation.titlePLOS ONE-
dc.citation.volume13-
dc.identifier.doi10.1371/journal.pone.0191740-
dc.citation.startPage1-
dc.citation.endPage20-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2016:23.4375-
dc.subject.keywordPro21717-
dc.subject.keywordPseudoalteromonas arctica PAMC 21717-
dc.subject.keywordX-ray crystallography-
dc.subject.keywordcrystal structure-
dc.subject.keywordserine protease-
dc.identifier.localId2018-0007-
dc.identifier.scopusid2-s2.0-85042348760-
dc.identifier.wosid000425604300015-
Appears in Collections  
2018-2018, Polar Genomics 101 Project: Genome analysis of polar organisms and establishment of application platform (18-18) / Kim, Jin-Hyoung
2017-2018, Polar Genomics 101 Project: Genome analysis of polar organisms and establishment of application platform (17-18) / Park, Hyun
2016-2018, Cryo-Biotech (16-18) / Yim, Joung Han; Han, Se Jong
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