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Spectroscopy
Volume 24 (2010), Issue 3-4, Pages 339-341
http://dx.doi.org/10.3233/SPE-2010-0449

Unusual structural characteristics of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA

S. Khrapunov,1,2 H. Cheng,1 S. Hegde,1 J. Blanchard,1 and M. Brenowitz1,2

1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA
2Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 104161, USA

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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.