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==Crystal structure of S-Adenosylmethionine synthase from Sulfolobus solfataricus complexed with SAM and PPi== | ==Crystal structure of S-Adenosylmethionine synthase from Sulfolobus solfataricus complexed with SAM and PPi== | ||
<StructureSection load='4l7i' size='340' side='right' caption='[[4l7i]], [[Resolution|resolution]] 2.19Å' scene=''> | <StructureSection load='4l7i' size='340' side='right' caption='[[4l7i]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mat, SSO0199 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mat, SSO0199 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l7i RCSB], [http://www.ebi.ac.uk/pdbsum/4l7i PDBsum]</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=4l7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7i OCA], [http://pdbe.org/4l7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l7i RCSB], [http://www.ebi.ac.uk/pdbsum/4l7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l7i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4l7i" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:25, 11 August 2016
Crystal structure of S-Adenosylmethionine synthase from Sulfolobus solfataricus complexed with SAM and PPiCrystal structure of S-Adenosylmethionine synthase from Sulfolobus solfataricus complexed with SAM and PPi
Structural highlights
Publication Abstract from PubMedSMNF: Methionine adenosyltransferase (MAT) is a family of enzymes that utilizes ATP and methionine to produce S-adenosylmethionine (AdoMet), the most crucial methyl donor in the biological methylation of biomolecules and bioactive natural products. Here, we report that the MAT from Sulfolobus solfataricus (sMAT), an enzyme from a poorly explored class of the MAT family, has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP. To investigate the molecular basis for AdoMet analog production, we have crystallized the sMAT in the AdoMet bound, S-adenosylethionine (AdoMet) bound, and unbound forms. Notably, among these structures, the AdoEth-bound form offers the first MAT structure containing a non-native product and cumulatively, these structures add new structural insight into the MAT family and allow for detailed active site comparison with its homologs in E. coli and human. As a thermostable MAT structure from archaea, the structures herein also provide as a basis for future engineering to potentially broaden AdoMet analog production as reagents for methyltransferase-catalyzed 'alkylrandomization' and/or the study of methylation in the context of biological processes. STRUCTURED DIGITAL ABSTRACT: sMAT and sMAT bind by x-ray crystallography (View interaction). Understanding Molecular Recognition of Promiscuity of Thermophilic Methionine Adenosyltransferase, sMAT from Sulfolobus solfataricus.,Wang F, Singh S, Zhang J, Huber TD, Helmich KE, Sunkara M, Hurley KA, Goff RD, Bingman CA, Morris AJ, Thorson JS, Phillips GN Jr FEBS J. 2014 Mar 20. doi: 10.1111/febs.12784. PMID:24649856[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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