CryoEM structure of full-length dimeric ClbP
Ontology highlight
ABSTRACT:
SUBMITTER: Richard Michael Walsh Jr
PROVIDER: EMPIAR-11422 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis of colibactin activation by the ClbP peptidase.
Velilla José A JA Volpe Matthew R MR Kenney Grace E GE Walsh Richard M RM Balskus Emily P EP Gaudet Rachelle R
Nature chemical biology 20221017 2
Colibactin, a DNA cross-linking agent produced by gut bacteria, is implicated in colorectal cancer. Its biosynthesis uses a prodrug resistance mechanism: a non-toxic precursor assembled in the cytoplasm is activated after export to the periplasm. This activation is mediated by ClbP, an inner-membrane peptidase with an N-terminal periplasmic catalytic domain and a C-terminal three-helix transmembrane domain. Although the transmembrane domain is required for colibactin activation, its role in cata ...[more]
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