8ajp
From Proteopedia
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(New page: '''Unreleased structure''' The entry 8ajp is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Halogen methyl transferase from Paraburkholderia xenovorans at 1.8 A in complex with SAH== | |
| + | <StructureSection load='8ajp' size='340' side='right'caption='[[8ajp]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ajp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraburkholderia_xenovorans Paraburkholderia xenovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AJP 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=8ajp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ajp OCA], [https://pdbe.org/8ajp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ajp RCSB], [https://www.ebi.ac.uk/pdbsum/8ajp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ajp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q145N6_PARXL Q145N6_PARXL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Late-stage methylation is a key technology in the development of pharmaceutical compounds. Methyltransferase biocatalysis may provide powerful options to insert methyl groups into complex molecules with high regio- and chemo-selectivity. The challenge of a large-scale application of methyltransferases is their dependence on S-adenosylmethionine (SAM) as a stoichiometric, and thus exceedingly expensive co-substrate. As a solution to this problem, we and others have explored the use of methyl halides as reagents for in-situ regeneration of SAM. However, the need to handle volatile electrophiles such as methyl iodide (MeI) may also hamper applications at scale. As a more practical solution, we have now developed an enzyme-catalyzed process that affords regeneration of SAM with methyl toluene sulfonate. In this report we describe enzymes from the thiopurine methyltransferase family that accept sulfate- and sulfonate-based methyl donors to convert S-adenosylhomocysteine to SAM with efficiencies that rival MeI-based reactions. | ||
| - | + | Synthetic reagents for enzyme-catalyzed methylation.,Wen X, Leisinger F, Leopold V, Seebeck FP Angew Chem Int Ed Engl. 2022 Aug 21. doi: 10.1002/anie.202208746. PMID:35989225<ref>PMID:35989225</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8ajp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Paraburkholderia xenovorans]] | ||
| + | [[Category: Leisinger F]] | ||
| + | [[Category: Seebeck FP]] | ||
Current revision
Crystal structure of Halogen methyl transferase from Paraburkholderia xenovorans at 1.8 A in complex with SAH
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