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The 3D Solution Structure of the C Terminal Domain of Diphtheria Toxin Repressor: in the Free and Bound Forms

Diphtheria toxin repressor protein (DtxR) is a 226 amino acid protein that regulates the genes for iron uptake in Corynebacterium diphtheria and also regulates the Diphtheria toxin production. The known functions of this protein include binding divalent metals, dimerazation, and DNA binding. All these functions are accounted for by the N terminal domain of the protein. The C terminal domain was not well defined in early crystal structures but by 2000 both crystallography and NMR agreed that the C terminal domain has an SH3 like fold. This has led us to investigate the possible role of the C terminal domain as a "switch" for the activation of DtxR. We propose that the C terminal domain binds to the linker between the N and C terminal domains of this protein and stabilizes the monomeric form of DtxR. Once this region is released by the C terminal domain the N terminal domain most have some sort of "folding event" then metal is bound and dimerazation can take place. To investigate the mechanism of binding to this linker region by the C terminal domain two protein constructs were made one from residues D144-L226 and the other from D110-L226. The first construct would be the Free form and the second would be the bound form thus given us insight into the mechanism of binding. Here the 3D solution structures of these two domains and a comparison is presented. / A Dissertation submitted to the Department of Chemistry in partial fulfillment of
the requirements for the degree of Doctor of Philosophy. / Degree Awarded: Spring Semester, 2003. / Date of Defense: January 27, 2003. / Diphtheria Toxin Repressor Protein (DtxR), Iron Uptake / Includes bibliographical references. / Timothy M. Logan, Professor Directing Dissertation; Piotr G. Fajer, Outside Committee Member; Michael Blaber, Committee Member; Naresh Dalal, Committee Member.

Identiferoai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_168850
ContributorsWylie, George P. (authoraut), Logan, Timothy M. (professor directing dissertation), Fajer, Piotr G. (outside committee member), Blaber, Michael (committee member), Dalal, Naresh (committee member), Department of Chemistry and Biochemistry (degree granting department), Florida State University (degree granting institution)
PublisherFlorida State University
Source SetsFlorida State University
LanguageEnglish, English
Detected LanguageEnglish
TypeText, text
Format1 online resource, computer, application/pdf

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