9h09
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Halide methyltransferase from Tulasnella calospora in complex with sinefungin and mesitylene sulfonate at room temperature== | |
| + | <StructureSection load='9h09' size='340' side='right'caption='[[9h09]], [[Resolution|resolution]] 2.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9h09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tulasnella_calospora_MUT_4182 Tulasnella calospora MUT 4182]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9H09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H09 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1IRH:2,4,6-trimethylbenzenesulfonic+acid'>A1IRH</scene>, <scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9h09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h09 OCA], [https://pdbe.org/9h09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h09 RCSB], [https://www.ebi.ac.uk/pdbsum/9h09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h09 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0C3QM78_9AGAM A0A0C3QM78_9AGAM] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:41381393</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9h09" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tulasnella calospora MUT 4182]] | ||
| + | [[Category: Bolotova SB]] | ||
| + | [[Category: Seebeck FP]] | ||
Current revision
Crystal structure of Halide methyltransferase from Tulasnella calospora in complex with sinefungin and mesitylene sulfonate at room temperature
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