Unknown

Dataset Information

0

Crystallization and preliminary X-ray diffraction analysis of mouse prostaglandin F2? synthase, AKR1B3.


ABSTRACT: Aldo-keto reductase 1B3 (AKR1B3) catalyzes the NADPH-dependent reduction of prostaglandin H(2) (PGH(2)), which is a common intermediate of various prostanoids, to form PGF(2?). AKR1B3 also reduces PGH(2) to PGD(2) in the absence of NADPH. AKR1B3 produced in Escherichia coli was crystallized in complex with NADPH by the sitting-drop vapour-diffusion method. The crystal was tetragonal, belonging to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 107.62, c = 120.76 Å. X-ray diffraction data were collected to 2.4 Å resolution at 100 K using a synchrotron-radiation source.

SUBMITTER: Takashima Y 

PROVIDER: S-EPMC3232157 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystallization and preliminary X-ray diffraction analysis of mouse prostaglandin F2α synthase, AKR1B3.

Takashima Yasuhide Y   Hatanaka Seika S   Mizohata Eiichi E   Nagata Nanae N   Fukunishi Yoshifumi Y   Matsumura Hiroyoshi H   Urade Yoshihiro Y   Inoue Tsuyoshi T  

Acta crystallographica. Section F, Structural biology and crystallization communications 20111130 Pt 12


Aldo-keto reductase 1B3 (AKR1B3) catalyzes the NADPH-dependent reduction of prostaglandin H(2) (PGH(2)), which is a common intermediate of various prostanoids, to form PGF(2α). AKR1B3 also reduces PGH(2) to PGD(2) in the absence of NADPH. AKR1B3 produced in Escherichia coli was crystallized in complex with NADPH by the sitting-drop vapour-diffusion method. The crystal was tetragonal, belonging to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 107.62, c = 120.76 Å. X-ray  ...[more]

Similar Datasets

| S-EPMC2374160 | biostudies-literature
| S-EPMC3660905 | biostudies-literature
| S-EPMC2935245 | biostudies-literature
| S-EPMC3944704 | biostudies-literature
| S-EPMC2496858 | biostudies-literature
| S-EPMC2339750 | biostudies-literature
| S-EPMC2917288 | biostudies-literature
| S-EPMC4188091 | biostudies-literature
| S-EPMC2222560 | biostudies-literature
| S-EPMC4259230 | biostudies-literature