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| | <StructureSection load='5af7' size='340' side='right'caption='[[5af7]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='5af7' size='340' side='right'caption='[[5af7]], [[Resolution|resolution]] 1.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5af7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Advenella_mimigardefordensis_dpn7 Advenella mimigardefordensis dpn7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AF7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5af7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Advenella_mimigardefordensis_DPN7 Advenella mimigardefordensis DPN7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AF7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-sulfinopropanoyl-CoA_desulfinase 3-sulfinopropanoyl-CoA desulfinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.13.1.4 3.13.1.4] </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=5af7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af7 OCA], [https://pdbe.org/5af7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5af7 RCSB], [https://www.ebi.ac.uk/pdbsum/5af7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5af7 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=5af7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af7 OCA], [http://pdbe.org/5af7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5af7 RCSB], [http://www.ebi.ac.uk/pdbsum/5af7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5af7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SPCAD_ADVMD SPCAD_ADVMD] Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite (PubMed:23354747, PubMed:26057676). Does not show dehydrogenase activity (PubMed:23354747). Involved in the degradation of 3,3'-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioesters (PTEs) (PubMed:23354747).<ref>PMID:23354747</ref> <ref>PMID:26057676</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-sulfinopropanoyl-CoA desulfinase]]
| + | [[Category: Advenella mimigardefordensis DPN7]] |
| - | [[Category: Advenella mimigardefordensis dpn7]] | + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cianci, M]] | + | [[Category: Cianci M]] |
| - | [[Category: Meijers, R]] | + | [[Category: Meijers R]] |
| - | [[Category: Schneider, T R]] | + | [[Category: Schneider TR]] |
| - | [[Category: Schuermann, M]] | + | [[Category: Schuermann M]] |
| - | [[Category: Steinbuechel, A]] | + | [[Category: Steinbuechel A]] |
| - | [[Category: 3-sulfinopropionyl-coenzyme some]]
| + | |
| - | [[Category: Acyl-coa dehydrogenase]]
| + | |
| - | [[Category: Desulfinase]]
| + | |
| - | [[Category: Flavin adenine dinucleotide]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
SPCAD_ADVMD Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite (PubMed:23354747, PubMed:26057676). Does not show dehydrogenase activity (PubMed:23354747). Involved in the degradation of 3,3'-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioesters (PTEs) (PubMed:23354747).[1] [2]
Publication Abstract from PubMed
3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase (AcdDPN7; EC 3.13.1.4) was identified during investigation of the 3,3'-dithiodipropionic acid (DTDP) catabolic pathway in the betaproteobacterium Advenella mimigardefordensis strain DPN7(T). DTDP is an organic disulfide and a precursor for the synthesis of polythioesters (PTEs) in bacteria, and is of interest for biotechnological PTE production. AcdDPN7 catalyzes sulfur abstraction from 3SP-CoA, a key step during the catabolism of DTDP. Here, the crystal structures of apo AcdDPN7 at 1.89 A resolution and of its complex with the CoA moiety from the substrate analogue succinyl-CoA at 2.30 A resolution are presented. The apo structure shows that AcdDPN7 belongs to the acyl-CoA dehydrogenase superfamily fold and that it is a tetramer, with each subunit containing one flavin adenine dinucleotide (FAD) molecule. The enzyme does not show any dehydrogenase activity. Dehydrogenase activity would require a catalytic base (Glu or Asp residue) at either position 246 or position 366, where a glutamine and a glycine are instead found, respectively, in this desulfinase. The positioning of CoA in the crystal complex enabled the modelling of a substrate complex containing 3SP-CoA. This indicates that Arg84 is a key residue in the desulfination reaction. An Arg84Lys mutant showed a complete loss of enzymatic activity, suggesting that the guanidinium group of the arginine is essential for desulfination. AcdDPN7 is the first desulfinase with an acyl-CoA dehydrogenase fold to be reported, which underlines the versatility of this enzyme scaffold.
3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold.,Schurmann M, Meijers R, Schneider TR, Steinbuchel A, Cianci M Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1360-72. doi:, 10.1107/S1399004715006616. Epub 2015 May 23. PMID:26057676[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schürmann M, Deters A, Wübbeler JH, Steinbüchel A. A novel 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis strain DPN7T acting as a key enzyme during catabolism of 3,3'-dithiodipropionic acid is a member of the acyl-CoA dehydrogenase superfamily. J Bacteriol. 2013 Apr;195(7):1538-51. PMID:23354747 doi:10.1128/JB.02105-12
- ↑ Schurmann M, Meijers R, Schneider TR, Steinbuchel A, Cianci M. 3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold. Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1360-72. doi:, 10.1107/S1399004715006616. Epub 2015 May 23. PMID:26057676 doi:http://dx.doi.org/10.1107/S1399004715006616
- ↑ Schurmann M, Meijers R, Schneider TR, Steinbuchel A, Cianci M. 3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold. Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1360-72. doi:, 10.1107/S1399004715006616. Epub 2015 May 23. PMID:26057676 doi:http://dx.doi.org/10.1107/S1399004715006616
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