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Type of Document Dissertation Author Wylie, George P URN etd-09042003-202335 Title The 3D Solution Structure Of The C Terminal Domain Of Diphtheria Toxin Repressor: In The Free And Bound Forms Degree Doctor of Philosophy Department Chemistry and Biochemistry, Department of Advisory Committee
Advisor Name Title Timothy M. Logan Committee Chair Michael Blaber Committee Member Naresh Dalal Committee Member Piotr G. Fajer Committee Member Keywords
- Diphtheria Toxin Repressor Protein (DtxR)
- Iron Uptake
Date of Defense 2003-06-01 Availability restricted Abstract Diphtheria toxin repressor protein (DtxR) is a 226 amino acid protein that regulates thegenes 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.
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