1nyb
From Proteopedia
(New page: 200px<br /><applet load="1nyb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nyb" /> '''SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI2...) |
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| - | [[Image:1nyb.gif|left|200px]]<br /><applet load="1nyb" size=" | + | [[Image:1nyb.gif|left|200px]]<br /><applet load="1nyb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nyb" /> | caption="1nyb" /> | ||
'''SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX'''<br /> | '''SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We determined the solution structure of a 22-amino-acid peptide from the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-21 Bacteriophage phi-21]. Full crystallographic information is available from [http:// | + | 1NYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-21 Bacteriophage phi-21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacteriophage phi-21]] | [[Category: Bacteriophage phi-21]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cilley, C | + | [[Category: Cilley, C D.]] |
| - | [[Category: Williamson, J | + | [[Category: Williamson, J R.]] |
[[Category: peptide-rna complex]] | [[Category: peptide-rna complex]] | ||
[[Category: transcription antitermination]] | [[Category: transcription antitermination]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:23 2008'' |
Revision as of 12:11, 21 February 2008
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SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX
Overview
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.
About this Structure
1NYB is a Single protein structure of sequence from Bacteriophage phi-21. Full crystallographic information is available from OCA.
Reference
Structural mimicry in the phage phi21 N peptide-boxB RNA complex., Cilley CD, Williamson JR, RNA. 2003 Jun;9(6):663-76. PMID:12756325
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