1NYB: SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX

Citation:
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.
PDB ID: 1NYBDownload
MMDB ID: 162360
PDB Deposition Date: 2003/2/12
Updated in MMDB: 2018/05
Experimental Method:
solution nmr
Source Organism:
Enterobacteria phage phi21
Similar Structures:
Molecular Components in 1NYB
Label Count Molecule
Protein (1 molecule)
1
Probable Regulatory Protein N
Molecule annotation
Nucleotide(1 molecule)
1
Boxb RNA
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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