Open AccessCrystallization of Escherichia coli CdtB, the biologically active subunit of cytolethal distending toxin
Author(s) -
Hontz Jill S.,
VillarLecumberri Maria T.,
Dreyfus Lawrence A.,
Yoder Marilyn D.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106002454
Subject(s) - cytolethal distending toxin , toxin , polyethylene glycol , protein subunit , escherichia coli , internalization , biological activity , microbiology and biotechnology , biology , chemistry , biochemistry , cell , in vitro , microbial toxins , gene
Cytolethal distending toxin (CDT) is a secreted protein toxin produced by several bacterial pathogens. The biologically active CDT subunit CdtB is an active homolog of mammalian type I DNase. Internalization of CdtB and subsequent translocation into the nucleus of target cells results in DNA‐strand breaks, leading to cell‐cycle arrest and apoptosis. CdtB crystals were grown using microbatch methods with polyethylene glycol 8000 as the precipitant. The CdtB crystals contain one molecule of MW 30.5 kDa per asymmetric unit, belong to space group P 2 1 2 1 2 1 and diffract to 1.72 Å.