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New page: left|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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== | ==SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX== | ||
We determined the solution structure of a 22-amino-acid peptide from the | <StructureSection load='1nyb' size='340' side='right'caption='[[1nyb]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nyb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_phi21 Enterobacteria phage phi21]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NYB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyb OCA], [https://pdbe.org/1nyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nyb RCSB], [https://www.ebi.ac.uk/pdbsum/1nyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nyb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/REGN_BPPH3 REGN_BPPH3] N protein regulates the transition from the early to the middle stage of lytic development. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Structural mimicry in the phage phi21 N peptide-boxB RNA complex.,Cilley CD, Williamson JR RNA. 2003 Jun;9(6):663-76. PMID:12756325<ref>PMID:12756325</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1nyb" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Cilley | <references/> | ||
[[Category: Williamson | __TOC__ | ||
</StructureSection> | |||
[[Category: Enterobacteria phage phi21]] | |||
[[Category: Large Structures]] | |||
[[Category: Cilley CD]] | |||
[[Category: Williamson JR]] | |||
Latest revision as of 21:53, 29 November 2023
SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEXSOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA COMPLEX
Structural highlights
FunctionREGN_BPPH3 N protein regulates the transition from the early to the middle stage of lytic development. Publication Abstract from PubMedWe 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. Structural mimicry in the phage phi21 N peptide-boxB RNA complex.,Cilley CD, Williamson JR RNA. 2003 Jun;9(6):663-76. PMID:12756325[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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