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• W2132357434 abstract "We determined the solution structure of a 22-amino-acid peptide from the amino-terminal domain of the bacteriophage [phis]21 N protein in complex with its cognate 24-mer boxB RNA hairpin using heteronuclear magnetic resonance spectroscopy. The N peptide binds as an α-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 [phis]21 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 [phis]21 boxB loop, in complex with the N peptide, is strikingly similar to the GNRA tetraloop-like folds of the related λ 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." @default.
• W2132357434 created "2016-06-24" @default.
• W2132357434 creator A5030717572 @default.
• W2132357434 creator A5074143608 @default.
• W2132357434 date "2003-06-01" @default.
• W2132357434 modified "2023-10-16" @default.
• W2132357434 title "Structural mimicry in the phage [phis]21 N peptide–<i>boxB</i> RNA complex" @default.
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• W2132357434 doi "https://doi.org/10.1261/rna.2189203" @default.
• W2132357434 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1370434" @default.
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• W2132357434 hasPublicationYear "2003" @default.
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