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Literature summary for 3.4.21.105 extracted from
- Micelle-catalyzed domain swapping in the GlpG rhomboid protease cytoplasmic domain (2014), Biochemistry, 53, 5907-5915.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P09391 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the cytoplasmic domain of the Escherichia coli GlpG rhomboid protease undergoes slow dimerization via domain swapping. Micromolar concentrations of micelles enhance monomer-dimer exchange rates by more than 1000fold. Detergents bearing a phosphocholine headgroup are true catalysts, with hexadecylphosphocholine reducing the 26 kcal/mol free energy barrier by more than 11 kcal/mol while preserving the 5 kcal/mol difference between monomer and dimer states. Catalysis involves the formation of a micelle-bound intermediate with a partially unfolded structure that is primed for domain swapping | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlpG | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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