1D6K

NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX

Summary for 1D6K

• Entry DOI: 10.2210/pdb1d6k/pdb
• Descriptor: 5S RRNA E-LOOP (5SE), RIBOSOMAL PROTEIN L25 (2 entities in total)
• Functional Keywords: protein-rna complex, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 22737.62

Authors

Stoldt, M.,Wohnert, J.,Ohlenschlager, O.,Gorlach, M.,Brown, L.R. (deposition date: 1999-10-14, release date: 1999-11-22, Last modification date: 2024-05-22)

Primary citation

Stoldt, M.,Wohnert, J.,Ohlenschlager, O.,Gorlach, M.,Brown, L.R.
The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition.
EMBO J., 18:6508-6521, 1999

PubMed Abstract: The structure of the complex between ribosomal protein L25 and a 37 nucleotide RNA molecule, which contains the E-loop and helix IV regions of the E-domain of Escherichia coli 5S rRNA, has been determined to an overall r.m.s. displacement of 1.08 A (backbone heavy atoms) by heteronuclear NMR spectroscopy (Protein Databank code 1d6k). The interacting molecular surfaces are bipartite for both the RNA and the protein. One side of the six-stranded beta-barrel of L25 recognizes the minor groove of the E-loop with very little change in the conformations of either the protein or the RNA and with the RNA-protein interactions occurring mainly along one strand of the E-loop duplex. This minor groove recognition module includes two parallel beta-strands of L25, a hitherto unknown RNA binding topology. Binding of the RNA also induces conversion of a flexible loop to an alpha-helix in L25, the N-terminal tip of which interacts with the widened major groove at the E-loop/helix IV junction of the RNA. The structure of the complex reveals that the E-domain RNA serves as a preformed docking partner, while the L25 protein has one preformed and one induced recognition module.

PubMed: 10562563
DOI: 10.1093/emboj/18.22.6508

Experimental method

SOLUTION NMR