The hypothetical Mycobacterium tuberculosis protein RV2302 (80 residues, MW = 8.6 kDa) has been characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. Size exclusion chromatography and NMR spectroscopy suggest that RV2302 is as a monomer is solution. Circular dichroism spectroscopy indicates the protein is structured in solution, but, irreversible unfolds upon heating with an inflection point of ~48°C. Using NMR based methods we determined the solution structure of RV2302. The protein contains a five strand, anti-parallel b-sheet core with one C-terminal a-helix (A65-A75) nestled against its side. Dali searches using the structure closest to the average structure did not identify any high similarities to any other known protein structure. Consequently, the structure of Rv2302 may potentially represent a novel protein fold.
Revised: August 31, 2006 |
Published: August 1, 2006
Citation
Buchko G.W., C.Y. Kim, T.C. Terwilliger, and M.A. Kennedy. 2006.Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis.Journal of Bacteriology 188, no. 16:5993-6001.PNNL-SA-46805.doi:10.1128/JB.00460-06