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| | <StructureSection load='6vcw' size='340' side='right'caption='[[6vcw]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='6vcw' size='340' side='right'caption='[[6vcw]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vcw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Barrel_medic Barrel medic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VCW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VCW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vcw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VCW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">11432371, MTR_7g102120, MtrunA17_Chr7g0264651 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3880 Barrel medic])</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=EDO:1,2-ETHANEDIOL'>EDO</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'>[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=6vcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vcw OCA], [https://pdbe.org/6vcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vcw RCSB], [https://www.ebi.ac.uk/pdbsum/6vcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vcw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6vcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vcw OCA], [http://pdbe.org/6vcw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vcw RCSB], [http://www.ebi.ac.uk/pdbsum/6vcw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vcw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G7L3W1_MEDTR G7L3W1_MEDTR]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] | + | [https://www.uniprot.org/uniprot/G7L3W1_MEDTR G7L3W1_MEDTR] 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 6vcw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6vcw" 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: Barrel medic]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Methionine adenosyltransferase]] | + | [[Category: Medicago truncatula]] |
| - | [[Category: Dauter, Z]] | + | [[Category: Dauter Z]] |
| - | [[Category: Ruszkowski, M]] | + | [[Category: Ruszkowski M]] |
| - | [[Category: Sekula, B]] | + | [[Category: Sekula B]] |
| - | [[Category: Sam synthase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
G7L3W1_MEDTR Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541]
Publication Abstract from PubMed
S-adenosylmethionine synthases (MATs) are responsible for production of S-adenosylmethionine, the cofactor essential for various methylation reactions, production of polyamines and phytohormone ethylene, etc. Plants have two distinct MAT types (I and II). This work presents the structural analysis of MATs from Arabidopsis thaliana (AtMAT1 and AtMAT2, both type I) and Medicago truncatula (MtMAT3a, type II), which, unlike most MATs, are dimers where three-domain subunits are sandwiched flat with one another. Although MAT types are very similar, their subunits are differently oriented within the dimer. Structural snapshots along the enzymatic reaction reveal the exact conformation of precatalytic methionine in the active site and show a binding niche, characteristic only for plant MATs, that may serve as a lock of the gate loop. Nevertheless, plants, in contrary to mammals, lack the MAT regulatory subunit, and the regulation of plant MAT activity is still puzzling. Our structures open a possibility of an allosteric activity regulation of type I plant MATs by linear compounds, like polyamines, which would tighten the relationship between S-adenosylmethionine and polyamine biosynthesis.
S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.,Sekula B, Ruszkowski M, Dauter Z Int J Biol Macromol. 2020 Feb 11. pii: S0141-8130(20)30238-5. doi:, 10.1016/j.ijbiomac.2020.02.100. PMID:32057875[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sekula B, Ruszkowski M, Dauter Z. S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula. Int J Biol Macromol. 2020 Feb 11. pii: S0141-8130(20)30238-5. doi:, 10.1016/j.ijbiomac.2020.02.100. PMID:32057875 doi:http://dx.doi.org/10.1016/j.ijbiomac.2020.02.100
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