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Title: Preliminary structural studies on the MtxX protein from Methanococcus jannaschii

Journal Article · · Acta Crystallographica. Section F
 [1]
  1. College of Pharmacy, Ewha Womans University, Seoul 120-750 (Korea, Republic of)

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, Vol. 64, Issue Pt 4; Other Information: PMCID: PMC2374245; PMID: 18391432; PUBLISHER-ID: fw5169; OAI: oai:pubmedcentral.nih.gov:2374245; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English