3EEB

Structure of the V. cholerae RTX cysteine protease domain

Summary for 3EEB

• Entry DOI: 10.2210/pdb3eeb/pdb
• Descriptor: RTX toxin RtxA, INOSITOL HEXAKISPHOSPHATE, SODIUM ION, ... (4 entities in total)
• Functional Keywords: v. cholerae, repeats-in-toxin, rtx, martx, cysteine protease, inositol hexakisphosphate, toxin
• Biological source: Vibrio cholerae
• Total number of polymer chains: 2
• Total formula weight: 46785.89

Authors

Lupardus, P.J.,Shen, A.,Bogyo, M.,Garcia, K.C. (deposition date: 2008-09-04, release date: 2008-10-21, Last modification date: 2024-02-21)

Primary citation

Lupardus, P.J.,Shen, A.,Bogyo, M.,Garcia, K.C.
Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain
Science, 322:265-268, 2008

PubMed 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.

PubMed: 18845756
DOI: 10.1126/science.1162403

Experimental method

X-RAY DIFFRACTION (2.1 Å)