5af7

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<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://www.rcsb.org/pdb/explore.do?structureId=5af7 RCSB], [http://www.ebi.ac.uk/pdbsum/5af7 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=5af7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5af7 RCSB], [http://www.ebi.ac.uk/pdbsum/5af7 PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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Revision as of 07:26, 26 August 2015

3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7T: crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold. Native crystal structure

5af7, resolution 1.89Å

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