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KMID : 0545120080180020283
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Journal of Microbiology and Biotechnology
2008 Volume.18 No. 2 p.283 ~ p.286
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Crystallization and Preliminary X-Ray Diffraction Analysis of 5,10- Methylenetetrahydrofolate Dehydrogenase/Cyclohydrolase from Thermoplasma acidophilum DSM 1728
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Kim Jae-Hee
Sung Min-Woo
Lee Eun-Hye
Nam Ki-Hyun
Hwang Kwang-Yeon
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Abstract
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The methylenetetrahydrofolate dehydrogenase/ cyclohydrolase (MTHFDC) from the thermoacidophilic archaeon Thermoplasma acidophilum is a 30.6 kDa molecular-mass enzyme that sequentially catalyzes the conversion of formyltetrahydrofolate to methylenetetrahydrofolate, with a preference for NADP as a cofactor, rather than NAD. In order to elucidate the functional and structural features of MTHFDC from archaeons at a molecular level, it was overexpressed in Escherichia coli and crystallized in the presence of its cofactor, NADP, at 295 K using polyethylene glycol (PEG) 4000 as a precipitant. The crystal is a member of the monoclinic space group P21, with the following unit cell parameters: a=66.333 A, b=52.868 A, c=86.099 A, and β= 97.570o, and diffracts to a resolution of at least 2.40 A at the synchrotron. Assuming a dimer in the crystallographic asymmetric unit, the calculated Matthews parameter (VM) was 2.44 A3/Da and the solvent content was 49.7%.
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KEYWORD
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Thermoplasma acidophilum, dehydrogenase, cyclohydrolase, crystallization
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