Structural highlights
Function
RL35A_PYRFU
Publication Abstract from PubMed
The ribosome consists of small and large subunits each comprised of dozens of proteins and RNA molecules. However, the functions of many of the individual protomers within the ribosome are still unknown. Here 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 beta-barrel analogous to the 'tRNA binding motif' fold. The structure of the P. furiosus RP-L35Ae presented here constitutes the first structural representative from this protein domain family. Proteins 2012. (c) 2012 Wiley Periodicals, Inc.
Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus.,Snyder DA, Aramini JM, Yu B, Huang YJ, Xiao R, Cort JR, Shastry R, Ma LC, Liu J, Rost B, Acton TB, Kennedy MA, Montelione GT Proteins. 2012 Mar 16. doi: 10.1002/prot.24071. PMID:22422653[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Snyder DA, Aramini JM, Yu B, Huang YJ, Xiao R, Cort JR, Shastry R, Ma LC, Liu J, Rost B, Acton TB, Kennedy MA, Montelione GT. Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus. Proteins. 2012 Mar 16. doi: 10.1002/prot.24071. PMID:22422653 doi:10.1002/prot.24071
