2KVC
Solution structure of the Mycobacterium tuberculosis protein Rv0543c, a member of the DUF3349 superfamily. Seattle Structural Genomics Center for Infectious Disease target MytuD.17112.a
Summary for 2KVC
Entry DOI | 10.2210/pdb2kvc/pdb |
NMR Information | BMRB: 16774 |
Descriptor | Putative uncharacterized protein (1 entity in total) |
Functional Keywords | tuberculosis, structural genomics, seattle structural genomics center for infectious disease, ssgcid, unknown function |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 11608.07 |
Authors | Buchko, G.W.,Kim, C.Y.,Terwilliger, T.C.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-03-12, release date: 2010-03-23, Last modification date: 2024-05-01) |
Primary citation | Buchko, G.W.,Phan, I.,Myler, P.J.,Terwilliger, T.C.,Kim, C.Y. Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c. Arch.Biochem.Biophys., 506:150-156, 2011 Cited by PubMed Abstract: 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, 11.3 kDa 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 α-helices, α1 (M1-Y16), α2 (P21-C33), α3 (S37-G52), α4 (G58-H65) and α5 (S72-G87), held together by a largely conserved group of hydrophobic amino acid side chains. Heteronuclear steady-state {¹H}-¹⁵N NOE, T₁, and T₂ 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 °C. While the biological function of Rv0543c is still unknown, the presence of DUF3349 proteins predominantly 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. PubMed: 21144816DOI: 10.1016/j.abb.2010.12.001 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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