9yce

Active site of MtgB, a glycine betaine methyltransferase from the MttB superfamily

spinqualitylabelsall models 9yce, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9yce is a 2 chain structure with sequence from Desulfitobacterium hafniense Y51. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: BET, EDO, IMD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MTGB_DESHY Methyltransferase able to methylate free cob(I)alamin in vitro, using glycine betaine as the methyl donor, yealding methylcobalamin (methylCbl) and dimethylglycine. In vivo, probably carries out the methylation of a corrinoid protein, likely the adjacently encoded DSY3155, with glycine betaine, to then supply methyl groups to tetrahydrofolate (THF) for ultimate conversion to carbon dioxide; oxidation of the methyl group would also provide reducing equivalents for anaerobic respiration. Thus, may function in the pathway that allows anaerobic methylotrophic growth of D.hafniense using glycine betaine. Cannot use quaternary amines such as carnitine and choline as substrates, nor tertiary amines such as dimethylglycine or trimethylamine. Publication Abstract from PubMed The MttB superfamily member MtgB catalyzes the methylation of a cognate corrinoid protein with glycine betaine, and representatives have been described from both bacteria and archaea. Here, we focused on MtgB from Desulfitobacterium hafniense, a protein for which a crystal structure had been previously obtained. We employed different programs to predict the binding of glycine betaine and identified a consensus binding site. The modelled binding site consisted of two aromatic residues, Y97 and F356, which are both proposed to interact with the quaternary amine portion of glycine betaine via pi:cation interactions. Additionally, two basic residues, H348 and R312, were proposed to interact with the carboxylate group. We carried out site-directed substitutions and subsequently tested the necessity of these residues for glycine betaine:cob(I)alamin methyltransferase activity. These experiments supported a role in catalysis for each residue, presumably in the placement of glycine betaine at the proper position for nucleophilic attack by the Co(I) ion of cobalamin. Subsequently, the structure of the glycine betaine-bound enzyme was obtained, confirming the interaction of these residues with glycine betaine. Other MttB superfamily members with specificity for different quaternary amines were modeled and compared with the glycine betaine-bound structure of MtgB. The nitrogen of each quaternary amine was brought within an average value of 1.8 A to each other, suggesting that members of the superfamily bring their methyl groups into nearly the same space within the TIM barrel prior to methyl group transfer to cob(I)alamin. Delineation of the active site of MtgB, a cobalamin-dependent glycine betaine methyltransferase.,Picking J, Li Y, Ticak T, Ferguson DJ, Hao B, Krzycki JA J Biol Chem. 2026 Jan 29;302(3):111216. doi: 10.1016/j.jbc.2026.111216. PMID:41617030 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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