6SK4
Methyltransferase MtgA from Desulfitobacterium hafniense in complex with methyl-tetrahydrofolate (P21)
Summary for 6SK4
| Entry DOI | 10.2210/pdb6sk4/pdb |
| Related | 6SJ8 |
| Descriptor | Methylcorrinoid:tetrahydrofolate methyltransferase, N-[4-({[(6S)-2-AMINO-4-HYDROXY-5-METHYL-5,6,7,8-TETRAHYDROPTERIDIN-6-YL]METHYL}AMINO)BENZOYL]-L-GLUTAMIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | anaerobic bacteria, glycine betaine metabolism, methyl transfer, cobalamin, tetrahydrofolate, transferase |
| Biological source | Desulfitobacterium hafniense Y51 |
| Total number of polymer chains | 4 |
| Total formula weight | 135963.00 |
| Authors | Badmann, T.,Groll, M. (deposition date: 2019-08-14, release date: 2019-09-25, Last modification date: 2024-01-24) |
| Primary citation | Badmann, T.,Groll, M. Structures in Tetrahydrofolate Methylation in Desulfitobacterial Glycine Betaine Metabolism at Atomic Resolution. Chembiochem, 21:776-779, 2020 Cited by PubMed Abstract: Enzymes orchestrating methylation between tetrahydrofolate (THF) and cobalamin (Cbl) are abundant among all domains of life. During energy production in Desulfitobacterium hafniense, MtgA catalyzes the methyl transfer from methylcobalamin (Cbl-CH ) to THF in the catabolism of glycine betaine (GB). Despite its lack of sequence identity with known structures, we could show that MtgA forms a homodimeric complex of two TIM barrels. Atomic crystallographic insights into the interplay of MtgA with THF as well as analysis of a trapped reaction intermediate (THF-CH ) reveal conformational rearrangements during the transfer reaction. Whereas residues for THF methylation are conserved, the binding mode for the THF glutamyl-p-aminobenzoate moiety (THF tail) is unique. Apart from snapshots of individual reaction steps of MtgA, structure-based mutagenesis combined with enzymatic activity assays allowed a mechanistic description of the methyl transfer between Cbl-CH and THF. Altogether, the THF-tail-binding motion observed in MtgA is unique compared to other THF methyltransferases and therefore contributes to the general understanding of THF-mediated methyl transfer. PubMed: 31518049DOI: 10.1002/cbic.201900515 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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