1a4t: Difference between revisions
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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== | ||
<StructureSection load='1a4t' size='340' side='right'caption='[[1a4t | <StructureSection load='1a4t' size='340' side='right'caption='[[1a4t]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a4t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1a4t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4T FirstGlance]. <br> | ||
</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=1a4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4t OCA], [https://pdbe.org/1a4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4t RCSB], [https://www.ebi.ac.uk/pdbsum/1a4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4t ProSAT]</span></td></tr> | </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=1a4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4t OCA], [https://pdbe.org/1a4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4t RCSB], [https://www.ebi.ac.uk/pdbsum/1a4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4t ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/REGN_BPP22 REGN_BPP22] N protein regulates the transition from the early to the middle stage of lytic development. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cai | [[Category: Salmonella virus P22]] | ||
[[Category: Frederick | [[Category: Cai Z]] | ||
[[Category: Gorin | [[Category: Frederick R]] | ||
[[Category: Hu | [[Category: Gorin AA]] | ||
[[Category: Kettani | [[Category: Hu W]] | ||
[[Category: Majumdar | [[Category: Kettani A]] | ||
[[Category: Patel | [[Category: Majumdar A]] | ||
[[Category: Ye | [[Category: Patel DJ]] | ||
[[Category: Ye X]] | |||
Latest revision as of 14:32, 22 November 2023
SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURESSOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES
Structural highlights
FunctionREGN_BPP22 N protein regulates the transition from the early to the middle stage of lytic development. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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