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

David A. Snyder, James M. Aramini, Bomina Yu, Yuanpeng J. Huang, Rong Xiao, John R. Cort, Ritu Shastry, Li Chung Ma, Jinfeng Liu, Burkhard Rost, Thomas B. Acton, Michael A. Kennedy, Gaetano T. Montelione

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1901-1906
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Issue number7
StatePublished - Jul 2012

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology


  • EF-Tu/eEF-1A
  • L35Ae
  • PF01247
  • Ribosomal protein
  • Solution NMR
  • Structural genomics
  • TRNA binding


Dive into the research topics of 'Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus'. Together they form a unique fingerprint.

Cite this