Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 DOI10.2210/pdb2kvc/pdb
NMR InformationBMRB: 16774
DescriptorPutative uncharacterized protein (1 entity in total)
Functional Keywordstuberculosis, structural genomics, seattle structural genomics center for infectious disease, ssgcid, unknown function
Biological sourceMycobacterium tuberculosis
Total number of polymer chains1
Total formula weight11608.07
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 citationBuchko, 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: 21144816
DOI: 10.1016/j.abb.2010.12.001
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227344

數據於2024-11-13公開中

PDB statisticsPDBj update infoContact PDBjnumon