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Entry ID KPDC_2018_0096
Entry Title X-ray diffraction data of PbAcE
Abstract Cold-active acetyl xylan esterases allow for reduced bioreactor heating costs in bioenergy production. Here, we isolated and characterized a cold-active acetyl xylan esterase (PbAcE) from the psychrophilic soil microbe Paenibacillus sp. R4. The enzyme reversibly hydrolyzes glucose penta-acetate and xylan acetate, alternatively producing acetyl xylan from xylan, and it shows higher activity at 4°C than at 25°C. We solved the crystal structure of PbAcE at 2.1-Å resolution to investigate its active site and the reason for its low-temperature activity. Structural analysis showed that PbAcE forms a hexamer with a central substrate binding tunnel, and the inter-subunit interactions are relatively weak compared with those of its mesophilic and thermophilic homologs. PbAcE also has a shorter loop and different residue composition in the β4–α3 and β5–α4 regions near the substrate binding site. Flexible subunit movements and different active site loop conformations may enable the strong low-temperature activity and broad substrate specificity of PbAcE. In addition, PbAcE was found to have strong activity against antibiotic compound substrates, such as cefotaxime and 7-amino cephalosporanic acid (7-ACA). In conclusion, the PbAcE structure and our biochemical results provide the first example of a cold-active acetyl xylan esterase and a starting template for structure-based protein engineering.
Purpose This manuscript describes the thorough characterization of a new member of the C7 family of carbohydrate esters, specifically the acetyl xylan esterase (AXE) from Paenibacillus sp (PbAcE). This is the first characterization of a cold-active AXE and the enzyme has a number of potential industrial applications.
Science Keyword
  • Biosphere > Ecological Dynamics > Community Dynamics > Biodiversity Functions
ISO Topic Category
  • Biota
Investigator
  • Lee, Changwoo (Email: justay@kopri.re.kr)
  • Park, Sun-Ha (Email: psh@kopri.re.kr)
  • Lee, Jun Hyuck (Email: junhyucklee@kopri.re.kr)
Instrument
  • BL-5C (BL-5C beam line of the Pohang Accelerator Laboratory)
Platform
    Location
    • 포항가속기연구소 (PAL)
    Spatial Coverage
    • (Lat: 36°, Lon: 01' 24.7" S) ~ (Lat: 129°, Lon: 18' 56.6" E)
    Temporal Coverage
    • 2018-07-26 ~ 2018-07-26
    Project
    • PE18210 극지유전자원 기반 신규활성 항생제 후보 물질 발굴
    Create/Update Date Thursday, October 4, 2018
    Author Lee Changwoo (Email: justay@kopri.re.kr)
    Data Center Korea Polar Data Center (KPDC)
    Contact Point kpdc@kopri.re.kr, more information

    Korea Polar Data Center

    Korea Polar Research Institute

    26, Songdomirae-ro, Yeonsu-gu, Incheon, Korea

    kpdc@kopri.re.kr