27NV
E. coli DSCD
Summary for 27NV
| Entry DOI | 10.2210/pdb27nv/pdb |
| Descriptor | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (1 entity in total) |
| Functional Keywords | e. coli dscd, e2 complex, e. coli dihydrolipoamide succinyltransferase, transferase |
| Biological source | Escherichia coli BL21(DE3) |
| Total number of polymer chains | 1 |
| Total formula weight | 44069.28 |
| Authors | |
| Primary citation | Lim, B.,Kim, E.,Byun, J.,Kim, M.,Kim, H.J. Sulfate-compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain. Acta Crystallogr.,Sect.F, 82:362-368, 2026 Cited by PubMed 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. PubMed: 42751796DOI: 10.1107/S2053230X2600909X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.59 Å) |
Structure validation
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