TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic analysis of l-Arabinose isomerase from thermophilic Geobacillus kaustophilus
AU - Cao, Thinh Phat
AU - Choi, Jin Myung
AU - Lee, Sang Jae
AU - Lee, Yong Jik
AU - Lee, Sung Keun
AU - Jun, Youngsoo
AU - Lee, Dong Woo
AU - Lee, Sung Haeng
PY - 2014/1
Y1 - 2014/1
N2 - l-Arabinose isomerase (AI), which catalyzes the isomerization of l-Arabinose to l-ribulose, can also convert d-galactose to d-tagatose, a natural sugar replacer, which is of commercial interest in the food and healthcare industries. Intriguingly, mesophilic and thermophilic AIs showed different substrate preferences and metal requirements in catalysis and different thermostabilities. However, the catalytic mechanism of thermophilic AIs still remains unclear. Therefore, thermophilic Geobacillus kaustophilus AI (GKAI) was overexpressed, purified and crystallized, and a preliminary X-ray diffraction data set was obtained. Diffraction data were collected from a GKAI crystal to 2.70 Å resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 224.12, b = 152.95, c = 91.28 Å, β = 103.61°. The asymmetric unit contained six molecules, with a calculated Matthews coefficient of 2.25 Å3 Da-1 and a solvent content of 45.39%. The three-dimensional structure determination of GKAI is currently in progress by molecular replacement and model building.
AB - l-Arabinose isomerase (AI), which catalyzes the isomerization of l-Arabinose to l-ribulose, can also convert d-galactose to d-tagatose, a natural sugar replacer, which is of commercial interest in the food and healthcare industries. Intriguingly, mesophilic and thermophilic AIs showed different substrate preferences and metal requirements in catalysis and different thermostabilities. However, the catalytic mechanism of thermophilic AIs still remains unclear. Therefore, thermophilic Geobacillus kaustophilus AI (GKAI) was overexpressed, purified and crystallized, and a preliminary X-ray diffraction data set was obtained. Diffraction data were collected from a GKAI crystal to 2.70 Å resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 224.12, b = 152.95, c = 91.28 Å, β = 103.61°. The asymmetric unit contained six molecules, with a calculated Matthews coefficient of 2.25 Å3 Da-1 and a solvent content of 45.39%. The three-dimensional structure determination of GKAI is currently in progress by molecular replacement and model building.
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U2 - 10.1107/S2053230X13033724
DO - 10.1107/S2053230X13033724
M3 - Article
C2 - 24419630
AN - SCOPUS:84905392661
VL - 70
SP - 108
EP - 112
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
IS - 1
ER -