1AUU

SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES

Summary for 1AUU

• Entry DOI: 10.2210/pdb1auu/pdb
• Descriptor: SACY (1 entity in total)
• Functional Keywords: antitermination, rna binding domain, transcription regulation
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 12730.93

Authors

Kochoyan, M. (deposition date: 1997-09-02, release date: 1997-11-12, Last modification date: 2024-05-22)

Primary citation

Manival, X.,Yang, Y.,Strub, M.P.,Kochoyan, M.,Steinmetz, M.,Aymerich, S.
From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins.
EMBO J., 16:5019-5029, 1997

PubMed Abstract: SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction.

PubMed: 9305643
DOI: 10.1093/emboj/16.16.5019

Experimental method

SOLUTION NMR