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| <StructureSection load='6ltw' size='340' side='right'caption='[[6ltw]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='6ltw' size='340' side='right'caption='[[6ltw]], [[Resolution|resolution]] 1.65Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6ltw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryho Cryho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LTW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LTW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ltw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LTW FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHUDEA7_2650 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 CRYHO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></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=6ltw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ltw OCA], [https://pdbe.org/6ltw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ltw RCSB], [https://www.ebi.ac.uk/pdbsum/6ltw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ltw ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ltw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ltw OCA], [http://pdbe.org/6ltw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ltw RCSB], [http://www.ebi.ac.uk/pdbsum/6ltw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ltw ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/A0A0S4TKQ5_CRYHO A0A0S4TKQ5_CRYHO]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] | + | [https://www.uniprot.org/uniprot/A0A0S4TKQ5_CRYHO A0A0S4TKQ5_CRYHO] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6ltw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ltw" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Cryho]] | + | [[Category: Cryptosporidium hominis]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Methionine adenosyltransferase]]
| + | [[Category: Kuemmel D]] |
- | [[Category: Kuemmel, D]] | + | [[Category: Michailidou F]] |
- | [[Category: Michailidou, F]] | + | [[Category: Rentmeister A]] |
- | [[Category: Rentmeister, A]] | + | [[Category: Singh RK]] |
- | [[Category: Singh, R K]] | + | |
- | [[Category: Mutanat]]
| + | |
- | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0A0S4TKQ5_CRYHO Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541]
Publication Abstract from PubMed
Methylation and demethylation of DNA, RNA and proteins has emerged as a major regulatory mechanism. Studying the function of these modifications would benefit from tools for their site-specific inhibition and timed removal. S -Adenosyl-L-methionine (AdoMet) analogs in combination with methyltransferases (MTases) have proven useful to map or block and release MTase target sites, however their enzymatic generation has been limited to aliphatic groups at the sulfur atom. We engineered a SAM synthetase from Cryptosporidium hominis (PC-ChMAT) for efficient generation of AdoMet analogs with photocaging groups that are not accepted by any WT MAT reported to date. The crystal structure of PC-ChMAT at 1.87 A revealed how the photocaged AdoMet analog is accommodated and guided engineering of a thermostable MAT from Methanocaldococcus jannaschii . PC-MATs were compatible with DNA- and RNA MTases, enabling sequence-specific modification ("writing") of plasmid DNA and light-triggered removal ("erasing").
Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions.,Michailidou F, Klocker N, Cornelissen N, Singh RK, Peters A, Ovcharenko A, Kummel D, Rentmeister A Angew Chem Int Ed Engl. 2020 Oct 5. doi: 10.1002/anie.202012623. PMID:33017502[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Michailidou F, Klocker N, Cornelissen N, Singh RK, Peters A, Ovcharenko A, Kummel D, Rentmeister A. Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions. Angew Chem Int Ed Engl. 2020 Oct 5. doi: 10.1002/anie.202012623. PMID:33017502 doi:http://dx.doi.org/10.1002/anie.202012623
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