1nyb

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

Structural highlights 1nyb is a 2 chain structure with sequence from Enterobacteria phage phi21. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function REGN_BPPH3 N protein regulates the transition from the early to the middle stage of lytic development. Publication Abstract from PubMed 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. Structural mimicry in the phage phi21 N peptide-boxB RNA complex.,Cilley CD, Williamson JR RNA. 2003 Jun;9(6):663-76. PMID:12756325 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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