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Proteins. 2012 Jul;80(7):1901-6. doi: 10.1002/prot.24071. Epub 2012 Apr 16.

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

Author information

1
Department of Chemistry, College of Science and Health, William Paterson University, Wayne, New Jersey 07470, USA.

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.

PMID:
22422653
PMCID:
PMC3639469
DOI:
10.1002/prot.24071
[Indexed for MEDLINE]
Free PMC Article

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