Crystallization and preliminary X-ray diffraction analysis of 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728
- Authors
- Kim, Jae-Hee; Sung, Min-Woo; Lee, Eun Hye; Nam, Ki Hyun; Hwang, Kwang Yeon
- Issue Date
- 2월-2008
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Thermoplasma acidophilum; dehydrogenase; cyclohydrolase; crystallization
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.18, no.2, pp.283 - 286
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 18
- Number
- 2
- Start Page
- 283
- End Page
- 286
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/124131
- ISSN
- 1017-7825
- Abstract
- 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 P2(1), with the following unit cell parameters: a=66.333 angstrom, b=52.868 angstrom, c=86.099 angstrom, and beta= 97.570 degrees, and diffracts to a resolution of at least 2.40 angstrom at the synchrotron. Assuming a dimer in the crystallographic asymmetric unit, the calculated Matthews parameter (V-M) was 2.44 angstrom(3) /Da and the solvent content was 49.7%.
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