Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus.

Abstract

The ribosome consists of small and large subunits each composed of dozens of proteins and RNA molecules. However, the functions of many of the individual protomers within the ribosome are still unknown. In this article, we describe the solution NMR structure of the ribosomal protein RP-L35Ae from the archaeon Pyrococcus furiosus. RP-L35Ae is buried within the large subunit of the ribosome and belongs to Pfam protein domain family PF01247, which is highly conserved in eukaryotes, present in a few archaeal genomes, but absent in bacteria. The protein adopts a six-stranded anti-parallel β-barrel analogous to the "tRNA binding motif" fold. The structure of the P. furiosus RP-L35Ae presented in this article constitutes the first structural representative from this protein domain family.

DOI: 10.1002/prot.24071

Cite this paper

@article{Snyder2012SolutionNS, title={Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus.}, author={David A. Snyder and James M. Aramini and Bomina Yu and Yuanpeng Janet Huang and Rong Xiao and John R. Cort and Ritu Shastry and Li-Chung Ma and Jinfeng Liu and Burkhard Rost and Thomas B. Acton and Michael A Kennedy and Gaetano T. Montelione}, journal={Proteins}, year={2012}, volume={80 7}, pages={1901-6} }