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7p84
From Proteopedia
(Difference between revisions)
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==Crystal structure of L147A/I351A variant of S-adenosylmethionine synthetase from Methanocaldococcus jannaschii in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)== | ==Crystal structure of L147A/I351A variant of S-adenosylmethionine synthetase from Methanocaldococcus jannaschii in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)== | ||
| - | <StructureSection load='7p84' size='340' side='right'caption='[[7p84]]' scene=''> | + | <StructureSection load='7p84' size='340' side='right'caption='[[7p84]], [[Resolution|resolution]] 2.05Å' 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=7P84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P84 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7p84]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P84 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=7p84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p84 OCA], [https://pdbe.org/7p84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p84 RCSB], [https://www.ebi.ac.uk/pdbsum/7p84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p84 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=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=EU9:[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[(3R)-3-azanyl-4-oxidanyl-4-oxidanylidene-butyl]-[(2-nitrophenyl)methyl]sulfanium'>EU9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [https://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=7p84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p84 OCA], [https://pdbe.org/7p84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p84 RCSB], [https://www.ebi.ac.uk/pdbsum/7p84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p84 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/METK_METJA METK_METJA]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.<ref>PMID:10660563</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Methylation and demethylation of DNA, RNA and proteins constitutes a major regulatory mechanism in epigenetic processes. Investigations would benefit from the ability to install photo-cleavable groups at methyltransferase target sites that block interactions with reader proteins until removed by non-damaging light in the visible spectrum. Engineered methionine adenosyltransferases (MATs) have been exploited in cascade reactions with methyltransferases (MTases) to modify biomolecules with non-natural groups, including first evidence for accepting photo-cleavable groups. We show that an engineered MAT from Methanocaldococcus jannaschii (PC-MjMAT) is 308-fold more efficient at converting ortho-nitrobenzyl-(ONB)-homocysteine than the wildtype enzyme. PC-MjMAT is active over a broad range of temperatures and compatible with MTases from mesophilic organisms. We solved the crystal structures of wildtype and PC-MjMAT in complex with AdoONB and a red-shifted derivative thereof. These structures reveal that aromatic stacking interactions within the ligands are key to accommodating the photocaging groups in PC-MjMAT. The enlargement of the binding pocket eliminates steric clashes to enable AdoMet analogue binding. Importantly, PC-MjMAT exhibits remarkable activity on methionine analogues with red-shifted ONB-derivatives enabling photo-deprotection of modified DNA by visible light. | ||
| + | |||
| + | Visible-Light Removable Photocaging Groups Accepted by MjMAT Variant: Structural Basis and Compatibility with DNA and RNA Methyltransferases.,Peters A, Herrmann E, Cornelissen NV, Klocker N, Kummel D, Rentmeister A Chembiochem. 2021 Oct 4. doi: 10.1002/cbic.202100437. PMID:34606675<ref>PMID:34606675</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7p84" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cornelissen | + | [[Category: Methionine adenosyltransferase]] |
| - | [[Category: Herrmann E]] | + | [[Category: Cornelissen, N V]] |
| - | [[Category: Kuemmel D]] | + | [[Category: Herrmann, E]] |
| - | [[Category: Peters A]] | + | [[Category: Kuemmel, D]] |
| - | [[Category: Rentmeister A]] | + | [[Category: Peters, A]] |
| + | [[Category: Rentmeister, A]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:40, 19 January 2022
Crystal structure of L147A/I351A variant of S-adenosylmethionine synthetase from Methanocaldococcus jannaschii in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)
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