2AYJ

Solution structure of 50S ribosomal protein L40e from Sulfolobus solfataricus

Summary for 2AYJ

• Entry DOI: 10.2210/pdb2ayj/pdb
• Descriptor: 50S ribosomal protein L40e, ZINC ION (2 entities in total)
• Functional Keywords: zn-binding; beta-strand protein, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, translation
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 1
• Total formula weight: 6527.37

Authors

Wu, B.,Yee, A.,Lukin, J.,Lemak, A.,Semesi, A.,Ramelot, T.,Kennedy, M.,Edward, A.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2005-09-07, release date: 2006-08-22, Last modification date: 2024-05-22)

Primary citation

Wu, B.,Lukin, J.,Yee, A.,Lemak, A.,Semesi, A.,Ramelot, T.A.,Kennedy, M.A.,Arrowsmith, C.H.
Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus
Protein Sci., 17:589-596, 2008

PubMed Abstract: The ribosomal protein L40E from archaeon Sulfolobus solfataricus is a component of the 50S ribosomal subunit. L40E is a 56-residue, highly basic protein that contains a C4 zinc finger motif, CRKC_X(10)_CRRC. Homologs are found in both archaea and eukaryotes but are not present in bacteria. Eukaryotic genomes encode L40E as a ubiquitin-fusion protein. L40E was absent from the crystal structure of euryarchaeota 50S ribosomal subunit. Here we report the three-dimensional solution structure of L40E by NMR spectroscopy. The structure of L40E is a three-stranded beta-sheet with a simple beta2beta1beta3 topology. There are two unique characteristics revealed by the structure. First, a large and ordered beta2-beta3 loop twists to pack across the one side of the protein. L40E contains a buried polar cluster comprising Lys19, Lys20, Cys22, Asn29, and Cys36. Second, the surface of L40E is almost entirely positively charged. Ten conserved basic residues are positioned on the two sides of the surface. It is likely that binding of zinc is essential in stabilizing the tertiary structure of L40E to act as a scaffold to create a broad positively charged surface for RNA and/or protein recognition.

PubMed: 18218710
DOI: 10.1110/ps.073273008

Experimental method

SOLUTION NMR