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Published on: December 20, 2010
Preliminary structural studies on the MtxX protein from Methanococcus jannaschii
1College of Pharmacy, Ewha Womans University, Seoul 120-750, Republic of Korea. dhshin55@ewha.ac.kr
Summary
Researchers studied the MtxX protein from Methanococcus jannaschii, a key enzyme in methane production. Structural analysis of this unique methyltransferase provides insights into its function in archaea.
Area of Science:
- Biochemistry
- Structural Biology
- Archaea Biology
Background:
- Methanococcus jannaschii produces methane via N(5)-methyltetrahydromethanopterin:coenzyme M methyltransferase (MTR).
- Some archaea possess the mtxXAH gene cluster, homologous to the mtr cluster.
- M. jannaschii uniquely contains both the mtr cluster and a single mtxX gene.
Purpose of the Study:
- To investigate the MtxX protein from M. jannaschii as a potentially unique methyltransferase family.
- To determine the protein's structure to understand its function-structure relationship.
Main Methods:
- Cloning, expression, and purification of the MtxX protein.
- Crystallization of the MtxX protein.
- Synchrotron X-ray diffraction data collection to 2.9 Å resolution from a selenomethionine-substituted crystal.
Main Results:
- The MtxX protein was successfully cloned, expressed, purified, and crystallized.
- Crystal data revealed a primitive hexagonal space group P6(1)22 with specific unit-cell parameters.
- A full structure determination is currently in progress.
Conclusions:
- The MtxX protein from M. jannaschii represents a distinct methyltransferase family.
- Structural determination will elucidate the protein's role in methanogenesis.
- This research contributes to understanding archaeal methane production pathways.
