Work

Crystallization ofEscherichia coliCdtB, the biologically active subunit of cytolethal distending toxin

Year: 2006

Type: article

Abstract: 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 P2(1)2(1)2(1) and diffract to 1.72 A.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309106002454

Authors: Jill S. Hontz, Maria T. Villar-Lecumberri, Lawrence A. Dreyfus, Marilyn D. Yoder

Institutions: University of Missouri–Kansas City, University of Kansas Medical Center

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funder: National Institute of Allergy and Infectious Diseases

Awards: G1709851379, Molecular Analysis of the Cytolethal Distending Toxin