Preliminary structural studies on the MtxX protein from Methanococcus jannaschii

Journal Article · Tue Apr 01 04:00:00 EDT 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309108007033· OSTI ID:22360514

In this study, the MtxX protein from M. jannaschii has been cloned, expressed, purified and crystallized. Methanococcus jannaschii has an mtr gene cluster expressing N{sup 5}-methyltetrahydromethanopterin:coenzyme M methyltransferase, which generates methane by reducing CO{sub 2} with H{sub 2} 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 P6{sub 1}22, 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.

• OSTI ID: 22360514
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALS
EXPLOSIONS
FORECASTING
METHANE
SPACE GROUPS
SYNCHROTRONS