Crystallization (Comment) | Organism |
---|---|
- |
Escherichia coli |
native protein, to 1.5 A resolution, and several derivatives. Structure reveals a dimeric protein that contains two positively charged, RNA-binding clefts along the surface of the protein. Each cleft contains a highly conserved aspartic acid located at its center. The structure suggests that a dimeric enzyme is required for binding transfer RNA and subsequent pseudouridine formation | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Escherichia coli |
dimer | crystallization data | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
pseudouridine synthase I | - |
Escherichia coli |