2LP6
Refined Solution NMR Structure of the 50S ribosomal protein L35Ae from Pyrococcus furiosus, Northeast Structural Genomics Consortium Target (NESG) PfR48
Summary for 2LP6
| Entry DOI | 10.2210/pdb2lp6/pdb |
| Related | 1SQR |
| NMR Information | BMRB: 6173 |
| Descriptor | 50S ribosomal protein L35Ae (1 entity in total) |
| Functional Keywords | structural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, ribosomal protein |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 1 |
| Total formula weight | 10826.71 |
| Authors | Snyder, D.A.,Aramini, J.M.,Yu, B.,Huang, Y.J.,Xiao, R.,Cort, J.R.,Shastry, R.,Ma, L.,Liu, J.,Rost, B.,Acton, T.B.,Kennedy, M.A.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2012-02-02, release date: 2012-02-15, Last modification date: 2024-05-15) |
| Primary citation | Snyder, D.A.,Aramini, J.M.,Yu, B.,Huang, Y.J.,Xiao, R.,Cort, J.R.,Shastry, R.,Ma, L.C.,Liu, J.,Rost, B.,Acton, T.B.,Kennedy, M.A.,Montelione, G.T. Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus. Proteins, 80:1901-1906, 2012 Cited by PubMed 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. PubMed: 22422653DOI: 10.1002/prot.24071 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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