Sulfate-compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain
Bison Lim, Eunji Kim, Jungeun Byun, Minjeong Kim, Hyo Jung Kim · 2026
Read Sulfate-compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain by Bison Lim, Eunji Kim, Jungeun Byun, Minjeong Kim, Hyo Jung Kim (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13629643.txt.
Description
Bison Lim and four colleagues report the crystal structure of a bacterial enzyme's catalytic domain, in a study from twenty twenty-six. The enzyme sits at the core of a multi-enzyme complex breaking down a metabolic intermediate. Its catalytic units assemble into trimers that expand into a twenty-four-part assembly. The crystals grew in a highly symmetric space group.
Near one lysine residue, the electron density fit a sulfate-like ion. That spot lies at the threefold junction between subunits of the trimer. Comparison with earlier structures marks it as an oxyanion-sensitive hotspot. A nearby helix reaches toward the active site pocket. It sits shifted relative to other crystal forms of the same domain. The authors link the ion density, the junction, and helix positioning within the assembly. The structure frames how local chemistry may tune this enzyme core.
Catalog record
| CREATOR | Bison Lim, Eunji Kim, Jungeun Byun, Minjeong Kim, Hyo Jung Kim |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 24 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |