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Preliminary structural studies on the MtxX protein from Methanococcus jannaschii
- Preliminary structural studies on the MtxX protein from Methanococcus jannaschii
- Shin D.H.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications vol. 64, no. 4, pp. 300 - 303
- Document Type
- Methanococcus jannaschii has an mtr gene cluster expressing N 5-methyltetrahydromethanopterin:coenzyme M methyltransferase, which generates methane by reducing CO2 with H2 with concomitant energy production under strictly anaerobic conditions. Some methanogenic archaea also have an mtr gene-cluster homologue, the mtxXAH gene cluster. M. jannaschii has both an entire mtr gene cluster and a single mtxX gene instead of the whole mtxXAH gene cluster. A PSI-BLAST search, secondary-structure prediction and the absence of phosphotransacetylase activity in M. jannaschii strongly support the possibility that the MtxX protein constitutes a unique methyltransferase family. In this study, the MtxX protein from M. jannaschii has been cloned, expressed, purified and crystallized. Synchrotron data were collected to 2.9 Å from a crystal of selenomethionine-substituted MtxX protein. The crystal belonged to the primitive hexagonal space group P6122, with unit-cell parameters a = 54.9, b = 54.9, c = 341.1 Å, β = 120.0°. A full structure determination is under way in order to provide insight into the structure-function relationship of this protein. © International Union of Crystallography 2008.
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