1SDS

Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA

Summary for 1SDS

• Entry DOI: 10.2210/pdb1sds/pdb
• Descriptor: box H/ACA sRNA, 50S ribosomal protein L7Ae, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: protein-rna complex, protein-rna complex complex, protein/rna complex
• Biological source: Methanocaldococcus jannaschii
• Cellular location: Cytoplasm : P54066
• Total number of polymer chains: 6
• Total formula weight: 53146.17

Authors

Hamma, T.,Ferre-D'Amare, A. (deposition date: 2004-02-13, release date: 2004-05-18, Last modification date: 2024-02-14)

Primary citation

Hamma, T.,Ferre-D'Amare, A.
Structure of Protein L7Ae Bound to a K-Turn Derived from an Archaeal Box H/ACA sRNA at 1.8 A Resolution.
STRUCTURE, 12:893-903, 2004

PubMed Abstract: The archaeal RNA binding protein L7Ae and its eukaryotic homolog 15.5 kDa/Snu13 recognize K-turns. This structural motif is canonically comprised of two stems (one with tandem A.G base pairs, the other with Watson-Crick pairs) linked by an asymmetric internal loop. L7Ae recognizes conventional K-turns in ribosomal and box C/D RNAs but also binds specifically to some box H/ACA RNAs at terminal stem loops. These have the A.G paired stem, but lack the Watson-Crick stem. The structure of Methanococcus jannaschii L7Ae bound to a symmetric duplex RNA without Watson-Crick stems demonstrates how a binding site for this component of diverse ribonucleoprotein complexes can be constructed with only the A.G stem and the loop. The RNA adopts a functional conformation with the aid of a base triple and tight binding of divalent cations. Comparison with the 15.5 kDa/Snu13-RNA complex structure suggests why the eukaryotic homolog does not recognize terminal stem loop L7Ae binding sites.

PubMed: 15130481
DOI: 10.1016/j.str.2004.03.015

Experimental method

X-RAY DIFFRACTION (1.8 Å)