Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 4 (April 2008)

crystallization communications

Acta Cryst. (2008). F64, 300-303 [ doi:10.1107/S1744309108007033 ]

Preliminary structural studies on the MtxX protein from Methanococcus jannaschii

D. H. Shin

Abstract: Methanococcus jannaschii has an mtr gene cluster expressing N⁵-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, [beta] = 120.0°. A full structure determination is under way in order to provide insight into the structure-function relationship of this protein.

Keywords: MtxX; Methanococcus jannaschii.