5YL7
Proteases from Pseudoalteromonas arctica PAMC 21717 (Pro21717)
Summary for 5YL7
| Entry DOI | 10.2210/pdb5yl7/pdb |
| Descriptor | Pseudoalteromonas arctica PAMC 21717, Copurified unknown peptide, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | serine protease, psychrophilic bacterium, pseudoalteromonas arctica, hydrolase |
| Biological source | Pseudoalteromonas arctica More |
| Total number of polymer chains | 2 |
| Total formula weight | 35257.05 |
| Authors | |
| Primary citation | 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 Cited by 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: 29466378DOI: 10.1371/journal.pone.0191740 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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