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

TitleSolution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus.
Publication TypeJournal Article
Year of Publication2012
AuthorsSnyder, DA, Aramini, JM, Yu, B, Huang, YJ, Xiao, R, Cort, JR, Shastry, R, Ma, L-C, Liu, J, Rost, B, Acton, TB, Kennedy, MA, Montelione, GT
Date Published2012 Jul
KeywordsAmino Acid Sequence, Archaeal Proteins, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Pyrococcus furiosus, Recombinant Proteins, Ribosomal Proteins, Sequence Alignment, Static Electricity

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.

Alternate JournalProteins
PubMed ID22422653
PubMed Central IDPMC3639469
Grant ListU54 GM094597 / GM / NIGMS NIH HHS / United States