EC Number   |
Protein Variants |
Reference |
|---|
   2.7.7.8 | more |
C-terminal KH/S1 domain truncated mutant, crystallization data. Mutant binds and cleaves RNA less efficiently with an 8fold reduced binding affinity and forms a less stable trimer. Mutation of Arg-residues in the central channel neck region produces defective enzymes that either bind and cleave RNA less efficiently or generate longer cleaved oligonucleotide products |
690030 |
| 2.7.7.8 | S441A |
catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure |
-, 760484 |
| 2.7.7.8 | S442A |
catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure |
-, 760484 |
| 2.7.7.8 | S443A |
catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure |
-, 760484 |
| 2.7.7.8 | DELTA549-709 |
complementation of growth defect at 15°C of host strain |
672449 |
| 2.7.7.8 | V304A/V305D |
complementation of growth defect at 15°C of host strain |
672449 |
| 2.7.7.8 | W233Stop |
complementation of growth defect at 15°C of host strain |
672449 |
| 2.7.7.8 | P98L |
complementation of growth defect at 15°C of host strain, forms of smaller colonies than host strain. Severe reduction of enzyme activity and increased PNPase expression levels |
672449 |
| 2.7.7.8 | V639D |
complementation of growth defect at 15°C of host strain, migrates slower than wild-type on SDS-PAGE, forms of smaller colonies than host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity |
672449 |
| 2.7.7.8 | E81D |
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity |
672449 |
