9h08

Crystal structure of Halide methyltransferase from Tulasnella calospora in complex with SAH at room temperature

spinqualitylabelsall models 9h08, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9h08 is a 1 chain structure with sequence from Tulasnella calospora MUT 4182. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.36Å Ligands: SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0C3QM78_9AGAM Publication Abstract from PubMed 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, S-adenosylmethionine (SAM). In this report, we describe a strain of Escherichia coli with a Short-Circuited SAM-Cycle (SCSC) that maintains its SAM pool exclusively by methylating S-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 in vivo methylation of SAH. We exploited this organism for the optimization of SAH-methylating enzymes by in vivo 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. Short-Circuiting the SAM-Cycle in Escherichia coli.,Li Z, Wen X, Bolotova SB, Seebeck FP J Am Chem Soc. 2025 Dec 11. doi: 10.1021/jacs.5c17370. PMID:41381393 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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