2kvc

Publication Abstract from PubMed

The first structure for a member of the DUF3349 (PF11829) family of proteins, Rv0543c from Mycobacterium tuberculosis, has been determined using NMR-based methods and some of its biophysical properties characterized. Rv0543c is a 100 residue, 11.3kDa protein that both size exclusion chromatography and NMR spectroscopy show to be a monomer in solution. The structure of the protein consists of a bundle of five alpha-helices, alpha1 (M1 - Y16), alpha2 (P21 - C33), alpha3 (S37 - G52), alpha4 (G58 - H65) and alpha5 (S72 - G87), held together by a largely conserved group of hydrophobic amino acid side chains. Heteronuclear steady-state {(1)H}-(15)N NOE, T(1), and T(2) values are similar through-out the sequence indicating that the backbones of the five helices are in a single motional regime. The thermal stability of Rv0543c, characterized by circular dichroism spectroscopy, indicates that Rv0543c irreversibly unfolds upon heating with an estimated melting temperature of 62.5 degrees C. While the biological function of Rv0543c is still unknown, the presence of DUF3349 proteins predominately in Mycobacterium and Rhodococcus bacterial species suggests that Rv0543 may have a biological function unique to these bacteria, and consequently, may prove to be an attractive drug target to combat tuberculosis.

Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c.,Buchko GW, Phan I, Myler PJ, Terwilliger TC, Kim CY Arch Biochem Biophys. 2011 Feb 15;506(2):150-6. Epub 2010 Dec 6. PMID:21144816^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.