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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]] 2.19&Aring;' scene=''>
<StructureSection load='4l7i' size='340' side='right'caption='[[4l7i]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l7i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L7I FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l7i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L7I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4l7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7i OCA], [https://pdbe.org/4l7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l7i RCSB], [https://www.ebi.ac.uk/pdbsum/4l7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l7i ProSAT]</span></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hpv|4hpv]], [[4k0b|4k0b]], [[4l2z|4l2z]]</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='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>
== Function ==
[https://www.uniprot.org/uniprot/METK_SACS2 METK_SACS2] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[HAMAP-Rule:MF_00136]
<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 4l7i" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4l7i" 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: Methionine adenosyltransferase]]
[[Category: Large Structures]]
[[Category: Sulso]]
[[Category: Saccharolobus solfataricus P2]]
[[Category: Bingman, C A]]
[[Category: Bingman CA]]
[[Category: Helmich, K E]]
[[Category: Helmich KE]]
[[Category: Hurley, K A]]
[[Category: Hurley KA]]
[[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis]]
[[Category: Phillips Jr GN]]
[[Category: Phillips, G N]]
[[Category: Singh S]]
[[Category: Singh, S]]
[[Category: Thorson JS]]
[[Category: Thorson, J S]]
[[Category: Wang F]]
[[Category: Wang, F]]
[[Category: Enzyme discovery for natural product biosynthesis]]
[[Category: Natpro]]
[[Category: PSI, Protein structure initiative]]
[[Category: Psi-biology]]
[[Category: Structural genomic]]
[[Category: Transferase]]

Revision as of 13:42, 14 December 2022

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

4l7i is a 2 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

METK_SACS2 Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[HAMAP-Rule:MF_00136]

Publication Abstract from PubMed

SMNF: 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.

See Also

References

  1. 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. Understanding Molecular Recognition of Promiscuity of Thermophilic Methionine Adenosyltransferase, sMAT from Sulfolobus solfataricus. FEBS J. 2014 Mar 20. doi: 10.1111/febs.12784. PMID:24649856 doi:http://dx.doi.org/10.1111/febs.12784

4l7i, resolution 2.19Å

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