Article

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

Department of Chemistry, College of Science and Health, William Paterson University, Wayne, New Jersey 07470, USA.
Proteins Structure Function and Bioinformatics (impact factor: 3.39). 03/2012; 80(7):1901-6. DOI:10.1002/prot.24071 pp.1901-6
Source: 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.

0 0
 · 
0 Bookmarks
 · 
39 Views
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.

Keywords

archaeal genomes
 
archaeon Pyrococcus furiosus
 
dozens
 
eukaryotes
 
first structural representative
 
individual protomers
 
large subunits
 
P. furiosus RP-L35Ae
 
Pfam protein domain family PF01247
 
protein domain family
 
proteins
 
ribosomal protein RP-L35Ae
 
RNA molecules
 
RP-L35Ae
 
six-stranded anti-parallel β-barrel analogous
 
solution NMR structure
 
tRNA binding motif