Crystallization (Comment) | Organism |
---|---|
structure in complex with cofactor SAM, to 2.2 A resolution. RsmI consists of an N-terminal putative RNA-binding domain and a C-terminal catalytic domain with a Rossmann-like fold, and belongs to the class III MTase family. SAM is specifically bound into a negatively charged deep pocket formed by both domains by making extensive contacts. Residues Asp100 and Ala124 are vital for SAM-binding. A base-flipping mechanism of the substrate RNA is possible | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
A124L | complete loss of binding affinity, mutation abolishes the side chain-mediating H-bond with SAM | Escherichia coli |
D100K | complete loss of binding affinity, mutation abolishes the side chain-mediating H-bond with SAM | Escherichia coli |
F144A | binding affinities and entropy are moderately affected | Escherichia coli |
Y169A | binding affinity and enthalpy/entropy are very similar to that of the wild-type | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P67087 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
RsmI | - |
Escherichia coli |