View source for 5ahs


==3-Sulfinopropionyl-Coenzyme A (3SP-CoA) desulfinase from Advenella mimgardefordensis DPN7T: holo crystal structure with the substrate analog succinyl-CoA==
<StructureSection load='5ahs' size='340' side='right'caption='[[5ahs]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ahs]] is a 6 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=5AHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AHS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ahs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ahs OCA], [https://pdbe.org/5ahs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ahs RCSB], [https://www.ebi.ac.uk/pdbsum/5ahs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ahs ProSAT]</span></td></tr>
</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;">
== 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<ref>PMID:26057676</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ahs" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Advenella mimigardefordensis DPN7]]
[[Category: Large Structures]]
[[Category: Cianci M]]
[[Category: Meijers R]]
[[Category: Schneider TR]]
[[Category: Schuermann M]]
[[Category: Steinbuechel A]]