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Crystallization and preliminary X-ray diffraction analysis of 5,10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728.
J Microbiol Biotechnol. 2008 Feb; 18(2):283-6.JM

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 P21, with the following unit cell parameters: a=66.333 A, b=52.868 A, c=86.099 A, and beta= 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%.

Authors+Show Affiliations

Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18309272

Citation

Kim, Jae-Hee, et al. "Crystallization and Preliminary X-ray Diffraction Analysis of 5,10- Methylenetetrahydrofolate Dehydrogenase/cyclohydrolase From Thermoplasma Acidophilum DSM 1728." Journal of Microbiology and Biotechnology, vol. 18, no. 2, 2008, pp. 283-6.
Kim JH, Sung MW, Lee EH, et al. Crystallization and preliminary X-ray diffraction analysis of 5,10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728. J Microbiol Biotechnol. 2008;18(2):283-6.
Kim, J. H., Sung, M. W., Lee, E. H., Nam, K. H., & Hwang, K. Y. (2008). Crystallization and preliminary X-ray diffraction analysis of 5,10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728. Journal of Microbiology and Biotechnology, 18(2), 283-6.
Kim JH, et al. Crystallization and Preliminary X-ray Diffraction Analysis of 5,10- Methylenetetrahydrofolate Dehydrogenase/cyclohydrolase From Thermoplasma Acidophilum DSM 1728. J Microbiol Biotechnol. 2008;18(2):283-6. PubMed PMID: 18309272.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction analysis of 5,10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728. AU - Kim,Jae-Hee, AU - Sung,Min-Woo, AU - Lee,Eun Hye, AU - Nam,Ki Hyun, AU - Hwang,Kwang Yeon, PY - 2008/3/1/pubmed PY - 2008/7/9/medline PY - 2008/3/1/entrez SP - 283 EP - 6 JF - Journal of microbiology and biotechnology JO - J Microbiol Biotechnol VL - 18 IS - 2 N2 - 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 beta= 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%. SN - 1017-7825 UR - https://www.unboundmedicine.com/medline/citation/18309272/Crystallization_and_preliminary_X_ray_diffraction_analysis_of_510__methylenetetrahydrofolate_dehydrogenase/cyclohydrolase_from_Thermoplasma_acidophilum_DSM_1728_ DB - PRIME DP - Unbound Medicine ER -