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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cheng, Huiyong Khrapunov, Sergei Hegde, Subray Brenowitz, Michael Blanchard, John |
| Description | Author Affiliation: Khrapunov S ( Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.) |
| Abstract | The pentapeptide repeat is a recently discovered protein fold. Mycobacterium tuberculosis MfpA is a founding member of the pentapeptide repeat protein (PRP) family that confers resistance to the antibiotic fluoroquinolone by binding to DNA gyrase and inhibiting its activity. The size, shape, and surface potential of MfpA mimics duplex DNA. As an initial step in a comprehensive biophysical analysis of the role of PRPs in the regulation of cellular topoisomerase activity and conferring antibiotic resistance, we have explored the solution structure and refolding of MfpA by fluorescence spectroscopy, CD, and analytical centrifugation. A unique CD spectrum for the pentapeptide repeat fold is described. This spectrum reveals a native structure whose beta-strands and turns within the right-handed quadrilateral beta-helix that define the PRP fold differ from canonical secondary structure types. MfpA refolded from urea or guanidium by dialysis or dilution forms stable aggregates of monomers whose secondary and tertiary structure are not native. In contrast, MfpA refolded using a novel 'time-dependent renaturation' protocol yields protein with native secondary, tertiary, and quaternary structure. The generality of 'time-dependent renaturation' to other proteins and denaturation methods is discussed. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 52 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-12-26 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Metabolism Mycobacterium Tuberculosis Amino Acid Sequence Circular Dichroism DNA Topoisomerases, Type I Drug Resistance, Microbial Guanidine Chemistry Molecular Sequence Data Monomeric GTP-Binding Proteins Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Spectrometry, Fluorescence Urea Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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