8ajp
From Proteopedia
(Difference between revisions)
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==Crystal structure of Halogen methyl transferase from Paraburkholderia xenovorans at 1.8 A in complex with SAH== | ==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]]' scene=''> | + | <StructureSection load='8ajp' size='340' side='right'caption='[[8ajp]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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> | + | <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='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> | + | </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> | </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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8ajp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Paraburkholderia xenovorans]] | ||
[[Category: Leisinger F]] | [[Category: Leisinger F]] | ||
[[Category: Seebeck FP]] | [[Category: Seebeck FP]] | ||
Revision as of 19:38, 7 September 2022
Crystal structure of Halogen methyl transferase from Paraburkholderia xenovorans at 1.8 A in complex with SAH
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