[2014.5.26] We published a paper onBiochem. Biophys. Res. Commun.which reported the structure of an Archaea-specific ribosmal protein L46a.Ribosome is largely conserved in three domains of life, while some ribosomal proteins exist only in a domain, class, or genus. Three Archaea-specific ribosomal proteins were recently identified, and they have no sequence homology with other known proteins. L46a is the most conserved one in the three ribosomal proteins. We determined the solution structure of L46a fromSulfolobus solfataricusP2 using NMR spectroscopy. By searching structural homologues in PDB, we found that the structure of L46a represents a novel protein fold. Analysis of the electrostatic surface of L46a revealed a large postively charged surface which is the potential rRNA-binding site. Docking the structure of L46a into an electron microscopy map reported in a previous study identified a potential position of L46a on the ribosome.

We accomplished the study collaborated with researchers in University of Science and Technology Beijing and Institute of Biophysics, Chinese Academy of Sciences. Prof. Yingang Feng is the first author and the corresponding author. The work was supported by the National High Technology Research and Development Program of China and the National Natural Science Foundation of China.

NCBI PubMed 

Yingang Feng*, Xiaxia Song, Jinzhong Lin, Jinsong Xuan, Qiu Cui, Jinfeng Wang (2014) Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold.Biochem. Biophys. Res. Commun.In press. [Full text (Publisher website)]