KOPRI Repository

PsEst3, a new psychrophilic esterase from the Arctic bacterium Paenibacillus sp. R4: crystallization and X-ray crystallographic analysis

Cited 0 time in wos
Cited 0 time in scopus
Metadata Downloads
Title
PsEst3, a new psychrophilic esterase from the Arctic bacterium Paenibacillus sp. R4: crystallization and X-ray crystallographic analysis
Other Titles
북극 미생물 Paenibacillus sp R4 유래의 저온성 에스테라제 PsEst3: 결정화와 X-ray 결정 분석
Authors
Kim, Hyun
Park, Ae Kyung
Lee, Jun Hyuck
Shin, Seung Chul
Park, Hyun
Kim, Han-Woo
Subject
Biochemistry & Molecular Biology; Biophysics; Crystallography
Keywords
Artic bacteria; Paenibacillus sp R4; crystal structure; esterase; psychrophilic
Issue Date
2018-06
Citation
Kim, Hyun, et al. 2018. "PsEst3, a new psychrophilic esterase from the Arctic bacterium Paenibacillus sp. R4: crystallization and X-ray crystallographic analysis". ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 74(6): 367-372.
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 A ° resolution. The crystal was determined to belong to space group P4132 or P4332, with unit-cell parameters a = b = c = 145.33 A ° . Further crystallographic analysis needs to be conducted to investigate the structure and function of this esterase.
URI
https://repository.kopri.re.kr/handle/201206/10525
DOI
http://dx.doi.org/10.1107/S2053230X18007525
Files in This Item
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

    Browse