PsEst3, a new psychrophilic esterase from the Arctic bacterium Paenibacillus sp. R4: crystallization and X‐ray crystallographic analysis. Issue 6 (5th June 2018)

• Record Type: Journal Article
• Authors: Kim, Hyun; Park, Ae Kyung; Lee, Jun Hyuck; Shin, Seung Chul; Park, Hyun; Kim, Han-Woo
• Is Part Of: Acta crystallographica. Volume 74:Issue 6(2018:Jun.)
• Page Start: 367
• Page End: 372
• Publication Date: 2018-06-05
• Subjects: crystal structure -- esterase -- Paenibacillus sp. R4 -- psychrophilic -- Artic bacteria; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X18007525
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The psychrophilic esterase PsEst3 was successfully overexpressed using a psychrophilic chaperonin co‐expression system, and was cystallized using the vapour‐diffusion method. The X‐ray diffraction data were collected to 2.1 Å resolution. Abstract : Esterases are very useful biocatalysts in industry: they hydrolyze esters and split them into a carboxylic acid and an alcohol. The psychrophilic esterase PsEst3 was obtained from Paenibacillus sp. R4, which was isolated from the active layer of the permafrost in Council, Alaska. PsEst3 was successfully overexpressed using a psychrophilic chaperonin co‐expression system and was purified by nickel‐affinity and size‐exclusion chromatography. Recombinant PsEst3 was crystallized at 290 K using the hanging‐drop vapour‐diffusion method. X‐ray diffraction data were collected to 2.1 Å resolution. The crystal was determined to belong to space group P 41 32 or P43 32, with unit‐cell parameters a = b = c = 145.33 Å. Further crystallographic analysis needs to be conducted to investigate the structure and function of this esterase.