1nyb: Difference between revisions

Revision as of 15:11, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1NYB is a Single protein structure of sequence from Bacteriophage phi-21. Full crystallographic information is available from OCA.

ReferenceReference

Structural mimicry in the phage phi21 N peptide-boxB RNA complex., Cilley CD, Williamson JR, RNA. 2003 Jun;9(6):663-76. PMID:12756325

Page seeded by OCA on Thu Feb 21 14:11:23 2008

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OCA

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-[[Image:1nyb.gif|left|200px]]<br /><applet load="1nyb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nyb.gif|left|200px]]<br /><applet load="1nyb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nyb" />
 '''SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX'''<br />
 ==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.
+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==
-NYB 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NYB OCA].
+NYB 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==
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 [[Category: Bacteriophage phi-21]]
 [[Category: Single protein]]
-[[Category: Cilley, C.D.]]
+[[Category: Cilley, C D.]]
-[[Category: Williamson, J.R.]]
+[[Category: Williamson, J R.]]
 [[Category: peptide-rna complex]]
 [[Category: transcription antitermination]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:39:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:23 2008''