3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase fromAdvenella mimigardefordensisDPN7T: crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold
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Medientyp:
E-Artikel
Titel:
3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase fromAdvenella mimigardefordensisDPN7T: crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold
Erschienen:
International Union of Crystallography (IUCr), 2015
Erschienen in:Acta Crystallographica Section D Biological Crystallography
Sprache:
Nicht zu entscheiden
DOI:
10.1107/s1399004715006616
ISSN:
1399-0047
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase (Acd<jats:sub>DPN7</jats:sub>; EC 3.13.1.4) was identified during investigation of the 3,3′-dithiodipropionic acid (DTDP) catabolic pathway in the betaproteobacterium<jats:italic>Advenella mimigardefordensis</jats:italic>strain DPN7<jats:sup>T</jats:sup>. DTDP is an organic disulfide and a precursor for the synthesis of polythioesters (PTEs) in bacteria, and is of interest for biotechnological PTE production. Acd<jats:sub>DPN7</jats:sub>catalyzes sulfur abstraction from 3SP-CoA, a key step during the catabolism of DTDP. Here, the crystal structures of apo Acd<jats:sub>DPN7</jats:sub>at 1.89 Å resolution and of its complex with the CoA moiety from the substrate analogue succinyl-CoA at 2.30 Å resolution are presented. The apo structure shows that Acd<jats:sub>DPN7</jats:sub>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. Acd<jats:sub>DPN7</jats:sub>is the first desulfinase with an acyl-CoA dehydrogenase fold to be reported, which underlines the versatility of this enzyme scaffold.</jats:p>