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Dynamics and Assembly of the Cytolethal Distending Toxin by Xin Hu; C. Erec Stebbins is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The cytolethal distending toxin (CDT) is a widespread bacterial toxin that consists of an active subunit CdtB with nuclease activity and two ricin‐like lectin domains, CdtA and CdtC, that are involved in the delivery of CdtB into the host cell. The three subunits form a tripartite complex that is required to achieve the fully active holotoxin. In the present study we investigate the assembly and dynamic properties of the CDT holotoxin using molecular dynamics simulations and binding free energy calculations. The results have revealed that CdtB likely adopts a different conformation in the unbound state with a closed DNA binding site. The two characterized structural elements of the aromatic patch and groove on the CdtA and CdtC protein surfaces exhibit high mobility, and free energy calculations show that the heterodimeric complex CdtA‐CdtC, as well as the CdtA‐CdtB and CdtB‐CdtC sub‐complexes are less energetically stable as compared to the binding in the tripartite complex. Analysis of the dynamical cross‐correlation map reveals information on the correlated motions and long‐range interplay among the CDT subunits associated with complex formation. Finally, the estimat

Who reads Dynamics and Assembly of the Cytolethal Distending Toxin?

Author

Xin Hu; C. Erec Stebbins

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)