Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.
Doukov, T., Seravalli, J., Stezowski, J.J., Ragsdale, S.W.(2000) Structure 8: 817-830
- PubMed: 10997901 
- DOI: https://doi.org/10.1016/s0969-2126(00)00172-6
- Primary Citation of Related Structures:  
1F6Y - PubMed Abstract: 
Methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr), catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide center in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin. We report the first structure of a protein in this family.
Organizational Affiliation: 
Department of Chemistry, University of Nebraska-Lincoln, 68503, USA.