Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 74, Issue -, Pages 367-372Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X18007525
Keywords
crystal structure; esterase; Paenibacillus sp R4; psychrophilic; Artic bacteria
Funding
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT and Future Planning (MSIP) (application study on Arctic cold-active enzymes degrading organic carbon compounds
- NRF Grant) [NRF-2017M1A5A1013568]
- Korea Polar Research Institute (KOPRI) [PN17083, PN18082]
- Polar Genomics 101 Project: Genome Analysis of Polar Organisms and Establishment of Application Platform - KOPRI [PE18080]
- Korea Polar Research Institute of Marine Research Placement (KOPRI) [PE18080] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 angstrom resolution. The crystal was determined to belong to space group P4(1)32 or P4(3)32, with unit-cell parameters a=b=c=145.33 angstrom. Further crystallographic analysis needs to be conducted to investigate the structure and function of this esterase.
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