1a4t

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[[Image:1a4t.jpg|left|200px]]
[[Image:1a4t.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1a4t| PDB=1a4t | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4t OCA], [http://www.ebi.ac.uk/pdbsum/1a4t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a4t RCSB]</span>
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'''SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES'''
'''SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES'''
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[[Category: Patel, D J.]]
[[Category: Patel, D J.]]
[[Category: Ye, X.]]
[[Category: Ye, X.]]
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[[Category: bacteriophage transcriptional antitermination]]
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[[Category: Bacteriophage transcriptional antitermination]]
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[[Category: bent alpha-helical peptide]]
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[[Category: Bent alpha-helical peptide]]
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[[Category: gnra loop]]
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[[Category: Gnra loop]]
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[[Category: peptide-rna recognition]]
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[[Category: Peptide-rna recognition]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:48:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:22 2008''
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Revision as of 06:48, 2 May 2008

Template:STRUCTURE 1a4t

SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES


Overview

We have determined the solution structure of a 15-mer boxB RNA hairpin complexed with a 20-mer basic peptide of the N protein involved in bacteriophage P22 transcriptional antitermination. Complex formation involves adaptive binding with the N peptide adopting a bent alpha-helical conformation that packs tightly through hydrophobic and electrostatic interactions against the major groove face of the boxB RNA hairpin, orienting the open opposite face for potential interactions with host factors and/or RNA polymerase. Four nucleotides in the boxB RNA hairpin pentaloop form a stable GNRA like tetraloop structural scaffold on complex formation, allowing the looped out fifth nucleotide to make extensive hydrophobic contacts with the bound peptide. The guanidinium group of a key arginine is hydrogen-bonded to the guanine in a loop-closing sheared G.A mismatch and to adjacent backbone phosphates. The identified intermolecular contacts account for the consequences of N peptide and boxB RNA mutations on bacteriophage transcriptional antitermination.

About this Structure

1A4T is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.

Reference

Solution structure of P22 transcriptional antitermination N peptide-boxB RNA complex., Cai Z, Gorin A, Frederick R, Ye X, Hu W, Majumdar A, Kettani A, Patel DJ, Nat Struct Biol. 1998 Mar;5(3):203-12. PMID:9501914 Page seeded by OCA on Fri May 2 09:48:41 2008

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