1NYB

SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX

Summary for 1NYB

• Entry DOI: 10.2210/pdb1nyb/pdb
• Related: 1A4T
• Descriptor: BoxB RNA, Probable regulatory protein N (2 entities in total)
• Functional Keywords: peptide-rna complex, transcription antitermination, transcription-rna complex, transcription/rna
• Biological source: Enterobacteria phage phi21; More
• Total number of polymer chains: 2
• Total formula weight: 10245.57

Authors

Cilley, C.D.,Williamson, J.R. (deposition date: 2003-02-12, release date: 2003-06-24, Last modification date: 2024-05-22)

Primary citation

Cilley, C.D.,Williamson, J.R.
Structural mimicry in the phage phi21 N peptide-boxB RNA complex
RNA, 9:663-676, 2003

PubMed Abstract: We determined the solution structure of a 22-amino-acid peptide from the amino-terminal domain of the bacteriophage phi21 N protein in complex with its cognate 24-mer boxB RNA hairpin using heteronuclear magnetic resonance spectroscopy. The N peptide binds as an alpha-helix and interacts predominately with the major groove side of the 5' half of the boxB RNA stem-loop. This binding interface is defined by surface complementarity of polar and nonpolar interactions, and little sequence-specific recognition. The phi21 boxB loop (CUAACC) has hydrogen bond and backbone torsions typical of the "U-turn" motif, as well as base stacking of the last 4 nt, and a hydrogen bonded C:C pair closing the loop. The exposed face of the phi21 boxB loop, in complex with the N peptide, is strikingly similar to the GNRA tetraloop-like folds of the related lambda and P22 bacteriophage N peptide-boxB RNA complexes. The N peptide-boxB complexes of the various phage, while individually distinct, provide similar structural features for interactions with the Escherichia coli host factors to enable antitermination.

PubMed: 12756325
DOI: 10.1261/rna.2189203

Experimental method

SOLUTION NMR