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NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.

Abstract：

:The structure of the complex formed by the arginine-rich motif of the transcriptional antitermination protein N of phage lambda and boxB RNA was determined by heteronuclear magnetic resonance spectroscopy. A bent alpha helix in N recognizes primarily the shape and negatively charged surface of the boxB hairpin through multiple hydrophobic and ionic interactions. The GAAGA boxB loop forms a GNRA fold, previously described for tetraloops, which is essential for N binding. The fourth nucleotide of the loop extrudes from the GNRA fold to enable the E. coli elongation factor NusA to recognize the N protein/RNA complex. This structure reveals a new mode of RNA-protein recognition and shows how a small RNA element can facilitate a protein-protein interaction and thereby nucleate formation of a large ribonucleoprotein complex.

journal_name

Cell

journal_title

Cell

authors

Legault P,Li J,Mogridge J,Kay LE,Greenblatt J

doi

10.1016/s0092-8674(00)81579-2

subject

Has Abstract

pub_date

1998-04-17 00:00:00

pages

289-99

issue

2

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)81579-2

journal_volume

93

pub_type

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