Secondary and tertiary structural changes in gamma delta resolvase: comparison of the wild-type enzyme, the I110R mutant, and the C-terminal DNA binding domain in solution

Protein Science : a Publication of the Protein Society
B PanG P Mullen

Abstract

gamma delta Resolvase is a site-specific DNA recombinase (M(r) 20.5 kDa) in Escherichia coli that shares homology with a family of bacterial resolvases and invertases. We have characterized the secondary and tertiary structural behavior of the cloned DNA binding domain (DBD) and a dimerization defective mutant in solution. Low-salt conditions were found to destabilize the tertiary structure of the DBD dramatically, with concomitant changes in the secondary structure that were localized near the hinge regions between the helices. The molten tertiary fold appears to contribute significantly to productive DNA interactions and supports a mechanism of DNA-induced folding of the tertiary structure, a process that enables the DBD to adapt in conformation for each of the three imperfect palindromic sites. At high salt concentrations, the monomeric I110R resolvase shows a minimal perturbation to the three helices of the DBD structure and changes in the linker segment in comparison to the cloned DBD containing the linker. Comparative analysis of the NMR spectra suggest that the I110R mutant contains a folded catalytic core of approximately 60 residues and that the segment from residues 100 to 149 are devoid of regular structure in the I1...Continue Reading

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Citations

Jun 12, 2009·Nucleic Acids Research·Gautam DharReid C Johnson
Dec 13, 2006·Molecular Plant-microbe Interactions : MPMI·Harold J G Meijer, Francine Govers
Sep 24, 1999·Protein Science : a Publication of the Protein Society·M YoungS Highsmith
Jun 28, 2005·Biophysical Journal·Marcelo NöllmannW Marshall Stark
Mar 28, 1998·The Journal of Biological Chemistry·I Baskakov, D W Bolen
Jun 25, 2015·Microbiology Spectrum·Phoebe A Rice

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