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| | ==Methionine Adenosyltransferase== | | ==Methionine Adenosyltransferase== |
| - | <StructureSection load='4l4q' size='340' side='right' caption='[[4l4q]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4l4q' size='340' side='right'caption='[[4l4q]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l4q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermococcus_kodakaraensis"_atomi_et_al._2004 "thermococcus kodakaraensis" atomi et al. 2004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L4Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l4q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L4Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mat, metK, TK0545 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 "Thermococcus kodakaraensis" Atomi et al. 2004])</td></tr> | + | </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=4l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4q OCA], [https://pdbe.org/4l4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l4q RCSB], [https://www.ebi.ac.uk/pdbsum/4l4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4q ProSAT]</span></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>
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| - | <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=4l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4q OCA], [http://pdbe.org/4l4q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l4q RCSB], [http://www.ebi.ac.uk/pdbsum/4l4q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/METK_THEKO METK_THEKO]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP (By similarity). | + | [https://www.uniprot.org/uniprot/METK_THEKO METK_THEKO] Catalyzes the formation of S-adenosylmethionine from methionine and ATP (By similarity). |
| | <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 4l4q" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4l4q" 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: Thermococcus kodakaraensis atomi et al. 2004]] | + | [[Category: Large Structures]] |
| - | [[Category: Methionine adenosyltransferase]] | + | [[Category: Thermococcus kodakarensis]] |
| - | [[Category: Andexer, J N]] | + | [[Category: Andexer JN]] |
| - | [[Category: Einsle, O]] | + | [[Category: Einsle O]] |
| - | [[Category: Gerhardt, S]] | + | [[Category: Gerhardt S]] |
| - | [[Category: Schlesier, J]] | + | [[Category: Schlesier J]] |
| - | [[Category: Siegrist, J]] | + | [[Category: Siegrist J]] |
| - | [[Category: Cytoplasmic]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
METK_THEKO Catalyzes the formation of S-adenosylmethionine from methionine and ATP (By similarity).
Publication Abstract from PubMed
BACKGROUND: Methionine adenosyltransferases catalyse the synthesis of S-adenosylmethionine, a cofactor abundant in all domains of life. In contrast to the enzymes from bacteria and eukarya that show high sequence similarity, methionine adenosyltransferases from archaea diverge on the amino acid sequence level and only few conserved residues are retained. RESULTS: We describe the initial characterisation and the crystal structure of the methionine adenosyltransferase from the hyperthermophilic archaeon Thermococcus kodakarensis. As described for other archaeal methionine adenosyltransferases the enzyme is a dimer in solution and shows high temperature stability. The overall structure is very similar to that of the bacterial and eukaryotic enzymes described, with some additional features that might add to the stability of the enzyme. Compared to bacterial and eukaryotic structures, the active site architecture is largely conserved, with some variation in the substrate/product-binding residues. A flexible loop that was not fully ordered in previous structures without ligands in the active side is clearly visible and forms a helix that leaves an entrance to the active site open. CONCLUSIONS: The similar three-dimensional structures of archaeal and bacterial or eukaryotic methionine adenosyltransferases support that these enzymes share an early common ancestor from which they evolved independently, explaining the low similarity in their amino acid sequences. Furthermore, methionine adenosyltransferase from T. kodakarensis is the first structure without any ligands bound in the active site where the flexible loop covering the entrance to the active site is fully ordered, supporting a mechanism postulated earlier for the methionine adenosyltransferase from E. coli. The structure will serve as a starting point for further mechanistic studies and permit the generation of enzyme variants with different characteristics by rational design.
Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis.,Schlesier J, Siegrist J, Gerhardt S, Erb A, Blaesi S, Richter M, Einsle O, Andexer JN BMC Struct Biol. 2013 Oct 18;13:22. doi: 10.1186/1472-6807-13-22. PMID:24134203[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schlesier J, Siegrist J, Gerhardt S, Erb A, Blaesi S, Richter M, Einsle O, Andexer JN. Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis. BMC Struct Biol. 2013 Oct 18;13:22. doi: 10.1186/1472-6807-13-22. PMID:24134203 doi:http://dx.doi.org/10.1186/1472-6807-13-22
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