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| | <StructureSection load='3iwc' size='340' side='right'caption='[[3iwc]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3iwc' size='340' side='right'caption='[[3iwc]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3iwc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IWC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3iwc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IWC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SMM:S-ADENOSYLMETHIONINE+METHYL+ESTER'>SMM</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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=SMM:S-ADENOSYLMETHIONINE+METHYL+ESTER'>SMM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tlu|1tlu]], [[1tmi|1tmi]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">speH, TM_0655 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosylmethionine_decarboxylase Adenosylmethionine decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.50 4.1.1.50] </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=3iwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iwc OCA], [https://pdbe.org/3iwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iwc RCSB], [https://www.ebi.ac.uk/pdbsum/3iwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iwc ProSAT]</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=3iwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iwc OCA], [https://pdbe.org/3iwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iwc RCSB], [https://www.ebi.ac.uk/pdbsum/3iwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iwc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SPEH_THEMA SPEH_THEMA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Adenosylmethionine decarboxylase]] | |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bale, S]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Bale S]] |
| - | [[Category: Kavita, B]] | + | [[Category: Ealick SE]] |
| - | [[Category: Autocatalytic cleavage]] | + | [[Category: Kavita B]] |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Polyamine biosynthesis]]
| + | |
| - | [[Category: Pyruvate]]
| + | |
| - | [[Category: S-adenosyl-l-methionine]]
| + | |
| - | [[Category: Schiff base]]
| + | |
| - | [[Category: Spermidine biosynthesis]]
| + | |
| - | [[Category: Zymogen]]
| + | |
| Structural highlights
Function
SPEH_THEMA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The polyamines putrescine, spermidine and spermine are ubiquitous aliphatic cations and are essential for cellular growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. The crystal structures of AdoMetDC from humans and plants and of the AdoMetDC proenzyme from Thermotoga maritima have been obtained previously. Here, the crystal structures of activated T. maritima AdoMetDC (TmAdoMetDC) and of its complexes with S-adenosylmethionine methyl ester and 5'-deoxy-5'-dimethylthioadenosine are reported. The results demonstrate for the first time that TmAdoMetDC autoprocesses without the need for additional factors and that the enzyme contains two complete active sites, both of which use residues from both chains of the homodimer. The complexes provide insights into the substrate specificity and ligand binding of AdoMetDC in prokaryotes. The conservation of the ligand-binding mode and the active-site residues between human and T. maritima AdoMetDC provides insight into the evolution of AdoMetDC.
Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity.,Bale S, Baba K, McCloskey DE, Pegg AE, Ealick SE Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):181-9. Epub 2010, Jan 22. PMID:20124698[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bale S, Baba K, McCloskey DE, Pegg AE, Ealick SE. Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity. Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):181-9. Epub 2010, Jan 22. PMID:20124698 doi:10.1107/S090744490904877X
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