Dataset Information
Clostridium difficile binary toxin translocase CDTb tetradecamer in symmetric and asymmetric conformations
Ontology highlight
ABSTRACT:
SUBMITTER: Amédée des Georges
PROVIDER: EMPIAR-11703 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure of the cell-binding component of the <i>Clostridium difficile</i> binary toxin reveals a di-heptamer macromolecular assembly.
Proceedings of the National Academy of Sciences of the United States of America 20200102 2
Targeting <i>Clostridium difficile</i> infection is challenging because treatment options are limited, and high recurrence rates are common. One reason for this is that hypervirulent <i>C. difficile</i> strains often have a binary toxin termed the <i>C. difficile</i> toxin, in addition to the enterotoxins TsdA and TsdB. The <i>C. difficile</i> toxin has an enzymatic component, termed CDTa, and a pore-forming or delivery subunit termed CDTb. CDTb was characterized here using a combination of sing ...[more]
