Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain.
basic_science · Level V
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- Record sourced from PubMed, PMID 18845756.
- Also identified by DOI 10.1126/science.1162403 and PMC identifier 3272704.
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Abstract
Vibrio cholerae RTX (repeats in toxin) is an actin-disrupting toxin that is autoprocessed by an internal cysteine protease domain (CPD). The RTX CPD is efficiently activated by the eukaryote-specific small molecule inositol hexakisphosphate (InsP6), and we present the 2.1 angstrom structure of the RTX CPD in complex with InsP6. InsP6 binds to a conserved basic cleft that is distant from the protease active site. Biochemical and kinetic analyses of CPD mutants indicate that InsP6 binding induces an allosteric switch that leads to the autoprocessing and intracellular release of toxin-effector domains.
Medical subject headings
- Acyltransferases
- Bacterial Proteins
- Bacterial Toxins
- Cysteine Endopeptidases
- Guanosine 5'-O-(3-Thiotriphosphate)
- Phytic Acid
- Vibrio cholerae