9H07
Crystal structure of Halide methyltransferase from Tulasnella calospora in complex with SAH and mesitylene sulfonate at room temperature
This is a non-PDB format compatible entry.
Summary for 9H07
| Entry DOI | 10.2210/pdb9h07/pdb |
| Related | 9H04 9H05 9H06 |
| Descriptor | Methyltransferase domain-containing protein, S-ADENOSYL-L-HOMOCYSTEINE, 2,4,6-trimethylbenzenesulfonic acid, ... (4 entities in total) |
| Functional Keywords | methyltransferase, halide methyltransferase, transferase |
| Biological source | Tulasnella calospora MUT 4182 |
| Total number of polymer chains | 1 |
| Total formula weight | 28509.08 |
| Authors | Bolotova, S.B.,Seebeck, F.P. (deposition date: 2024-10-07, release date: 2025-12-24, Last modification date: 2026-01-07) |
| Primary citation | Li, Z.,Wen, X.,Bolotova, S.B.,Seebeck, F.P. Short-Circuiting the SAM-Cycle in Escherichia coli . J.Am.Chem.Soc., 147:47690-47700, 2025 Cited by PubMed Abstract: Enzyme-mediated transfer of methyl groups to specific nucleophilic functions on small metabolites, proteins, and nucleic acids is an essential activity in all known life forms. Most of these transferred methyl groups originate from the one-carbon metabolism through methyl-tetrahydrofolate-dependent methylation of homocysteine, followed by adenosylation of methionine to form the primary methyltransferase cofactor, -adenosylmethionine (SAM). In this report, we describe a strain of with a Short-Circuited SAM-Cycle (SCSC) that maintains its SAM pool exclusively by methylating -adenosylhomocysteine (SAH) using a synthetic methyl donor. Construction of this strain was made possible by the identification of an aryl sulfonate methyl ester as a biocompatible methyl donor and methyltransferases that accept this compound as substrate for methylation of SAH. We exploited this organism for the optimization of SAH-methylating enzymes by selection and to produce isotope-labeled natural products. Looking ahead, we anticipate that strains with SCSCs will open new possibilities for methyltransferase biocatalysis, natural product discovery, and bacterial metabolomics. PubMed: 41381393DOI: 10.1021/jacs.5c17370 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.41 Å) |
Structure validation
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