Application | Comment | Organism |
---|---|---|
analysis | development of a fluorescence-based binding assay for 30S-NpmA interaction | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
electrostatic interactions made by the NpmA beta2/3 linker collectively are critical for docking of NpmA on a conserved 16S rRNA tertiary surface. Other NpmA regions (beta5/beta6 and beta6/beta7 linkers) contain several residues critical for optimal positioning of A1408 but are largely dispensable for 30S binding. In a model for NpmA action, 30S binding and adoption of a catalytically competent state are distinct: docking on 16S rRNA via the beta2/3 linker necessarily precedes functionally critical 30S substrate-driven conformational changes elsewhere in NpmA | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
E184C | introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S and dissociates upon addition of SAM | Escherichia coli |
E188C | introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM | Escherichia coli |
K131C | introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutation blocks 30S-NpmA interaction | Escherichia coli |
S89C | introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | A8C927 | - |
- |