Unusual structural characteristics of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA

Issue title: From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 2 of 2

Article type: Research Article

Authors: Khrapunov, S. | Cheng, H. | Hegde, S. | Blanchard, J. | Brenowitz, M.

Affiliations: Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA

Note: [] Corresponding authors: S. Khrapunov and M. Brenowitz, Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 104161, USA. Tel.: +1 718 430 3180; Fax: +1 718 430 8565; E-mails: {khraps, brenowit}@einstein.yu.edu.

Abstract: The solution structure and refolding of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA was explored by fluorescence and circular dichroism spectroscopy. Our results show that MfpA exists in two stable structural forms which exclusively favor dimer or oligomer formation. The structural malleability of MfpA may provide a novel target for drug discovery.

Keywords: Protein structure, protein stability, drug resistance

DOI: 10.3233/SPE-2010-0449

Journal: Spectroscopy, vol. 24, no. 3-4, pp. 339-341, 2010