ArticleActa crystallographica. Section F, Structural biology communications2026
Sulfate-compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain.
Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The catalytic domain of Escherichia coli dihydrolipoamide succinyltransferase (EcDSCD), the E2 component of the 2-oxoglutarate dehydrogenase complex, forms the oligomeric core of the multi-enzyme assembly. Here, we report the crystal structure of EcDSCD determined in space group F432. The F432 crystal symmetry captures a compact trimeric building block and a symmetry-expanded 24-subunit assembly consistent with the octahedral architecture of the E2 catalytic core. Structural analysis revealed sulfate-compatible electron density near Lys196 at a crystallographic threefold intratrimeric junction. Comparison with previously reported EcDSCD structures suggests that this density marks a structurally relevant oxyanion-sensitive hotspot at the intratrimeric junction. Notably, the α1-helix is positioned adjacent to the Lys196-centered junction and extends towards the active-site pocket, where it adopts a shifted orientation relative to other EcDSCD crystal forms. These observations link sulfate-compatible density, the intratrimeric junction and α1-helix positioning within the EcDSCD 24-mer, providing a structural framework for understanding local oxyanion-sensitive features in the E2 catalytic core.
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