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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...

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Identifiers

PMID: 32320214
DOI: 10.1021/acs.biochem.9b01047
PMCID: PMC7260706

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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