1nyb
From Proteopedia
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SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX
Overview
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.
About this Structure
1NYB is a Single protein structure of sequence from Bacteriophage phi-21. Full crystallographic information is available from OCA.
Reference
Structural mimicry in the phage phi21 N peptide-boxB RNA complex., Cilley CD, Williamson JR, RNA. 2003 Jun;9(6):663-76. PMID:12756325
Page seeded by OCA on Tue Nov 20 22:39:26 2007
