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PDBsum entry 5af7
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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M.Schürmann,
R.Meijers,
T.R.Schneider,
A.Steinbüchel,
M.Cianci.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2015,
71,
1360-1372.
[DOI no: ]
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PubMed id
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Abstract
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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 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
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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