1a4t
From Proteopedia
(New page: 200px<br /><applet load="1a4t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4t" /> '''SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BO...) |
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| - | [[Image:1a4t.jpg|left|200px]]<br /><applet load="1a4t" size=" | + | [[Image:1a4t.jpg|left|200px]]<br /><applet load="1a4t" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the solution structure of a 15-mer boxB RNA hairpin | + | 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== | ==About this Structure== | ||
| - | 1A4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http:// | + | 1A4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cai, Z.]] | [[Category: Cai, Z.]] | ||
[[Category: Frederick, R.]] | [[Category: Frederick, R.]] | ||
| - | [[Category: Gorin, A | + | [[Category: Gorin, A A.]] |
[[Category: Hu, W.]] | [[Category: Hu, W.]] | ||
[[Category: Kettani, A.]] | [[Category: Kettani, A.]] | ||
[[Category: Majumdar, A.]] | [[Category: Majumdar, A.]] | ||
| - | [[Category: Patel, D | + | [[Category: Patel, D J.]] |
[[Category: Ye, X.]] | [[Category: Ye, X.]] | ||
[[Category: bacteriophage transcriptional antitermination]] | [[Category: bacteriophage transcriptional antitermination]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:57 2008'' |
Revision as of 09:40, 21 February 2008
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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 Yersinia phage py54. 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
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