Article
The Positively Charged Active Site of the Bacterial Toxin RelE Causes a Large Shift in the General Base pKa.
Biochemistry - 5 May 2020
Hiller David A, Dunican Brian F, Nallur Sunitha, Li Nan-Sheng, Piccirilli Joseph A, Strobel Scott A
Abstract excerpt
The bacterial toxin RelE cleaves mRNA in the ribosomal A site. Although it shares a global fold with other microbial RNases, the active site contains several positively charged residues instead of histidines and glutamates that are typical of ribonucleases. The pH dependences of wild-type and mutant RelE indicate it uses general acid-base catalysis, but either the general acid (proposed to be R81) or the general...
Topics
- Bacterial Toxins
- Biocatalysis
- Catalytic Domain
- Hydrogen-Ion Concentration
- Kinetics
- Models, Molecular
- Mutation
- RNA, Messenger