Dataset Information

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.

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.

SUBMITTER: Park HJ

PROVIDER: S-EPMC5821440 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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

Park Ha Ju HJ Lee Chang Woo CW Kim Dockyu D Do Hackwon H Han Se Jong SJ Kim Jung Eun JE Koo Bon-Hun BH Lee Jun Hyuck JH Yim Joung Han JH

PloS one 20180221 2

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 bacter ...[more]

PMID: 29466378

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Project description:Liquid laundry capsules have been involved in multiple poisoning incidents with young children in the home. There are a range of contributing factors for these incidents, including influences from industry, culture, home environments, and parenting/supervision. There also are influences from children's behaviour and decisions in reaction to potential hazards. Previous research examined the influence of capsule product appearance and colour on children's behaviour around hazardous household items, but little research examines the influence of product size. This research explored if differences in the size of liquid laundry capsules result in different levels of toddler interaction. We compared two commercially available capsule designs that are identical in physical appearance but differ in physical size. Our research was conducted using three studies: Study 1, forced-choice test in an out-of-context laboratory setting; Study 2, an ecologically-valid, simulated real-world setting replicating a home laundry cabinet with a container of capsules left open; and Study 3, a second ecologically-valid study replicating a home laundry cabinet, this time with a capsule left outside its container. Capsule interaction was measured by grasping choice among samples of 156 toddlers ages 9-36 months. The same sample was used for Studies 1 and 2, and a second identically sized sample recruited for Study 3. Results from Study 1 indicated toddlers selected the small (49.8% selection) and large (50.2%) capsule with nearly identical frequency. Study 2 largely replicated Study 1: Toddlers selected the small capsule or container of small capsules 26.8% of the time and the large capsule or container of large capsules 22.3% of the time. Study 3 also replicated previous findings: Toddlers selected the smaller capsule 18.0% of the time and the larger 19.2%. We discuss study results, which suggest no appreciable difference in toddler's grasping choice to smaller versus larger laundry capsules.

Dataset Information

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.

Publications

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

Similar Datasets

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