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Preliminary structural studies on the MtxX protein from Methanococcus jannaschii

Title
Preliminary structural studies on the MtxX protein from Methanococcus jannaschii
Authors
Shin D.H.
Ewha Authors
신동해
SCOPUS Author ID
신동해scopus
Issue Date
2008
Journal Title
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN
1744-3091JCR Link
Citation
vol. 64, no. 4, pp. 300 - 303
Indexed
SCOPUS WOS scopus
Abstract
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.
DOI
10.1107/S1744309108007033
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약학대학 > 약학과 > Journal papers
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