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1hji

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(New page: 200px<br /><applet load="1hji" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hji" /> '''BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA ...)
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[[Image:1hji.gif|left|200px]]<br /><applet load="1hji" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hji" />
 
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'''BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX'''<br />
 
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==Overview==
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==BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX==
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Nun protein from coliphage HK022 binds to phage boxB RNA and functions, in, contrast to phage lambda N protein, as a transcriptional terminator. The, basic Nun-(10-44) peptide contains the boxB RNA binding arginine rich, motif, ARM. The peptide binds boxB RNA and competes with the phage lambda, ARM peptide N-(1-36) as indicated by nuclear magnetic resonance (NMR), spectroscopy titrations. In two-dimensional nuclear Overhauser enhancement, spectroscopy experiments boxB RNA in complex with Nun-(20-44) exhibits the, same pattern of resonances as it does in complex with N peptides, containing the ARM, and we could show that Nun-(20-44) forms a bent, alpha-helix upon binding to the boxB RNA. The structure of the boxB, RNA-bound Nun-(20-44) was determined on the basis of 191 intra- and 30, intermolecular distance restraints. Ser-24 is anchored to the lower RNA, stem, and stacking of Tyr-39 and A7 is clearly experimentally indicated., Arg-28 shows numerous contacts to the RNA stem. Leu-22, Ile-30, Trp-33, Ile-37, and Leu-41 form a hydrophobic surface, which could be a, recognition site for additional host factors such as NusG. Such a, hydrophobic surface area is not present in N-(1-36) bound to boxB RNA.
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<StructureSection load='1hji' size='340' side='right'caption='[[1hji]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hji]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_HK022 Escherichia virus HK022] and [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hji OCA], [https://pdbe.org/1hji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hji RCSB], [https://www.ebi.ac.uk/pdbsum/1hji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hji ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VNUN_BPHK0 VNUN_BPHK0]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nun protein from coliphage HK022 binds to phage boxB RNA and functions, in contrast to phage lambda N protein, as a transcriptional terminator. The basic Nun-(10-44) peptide contains the boxB RNA binding arginine rich motif, ARM. The peptide binds boxB RNA and competes with the phage lambda ARM peptide N-(1-36) as indicated by nuclear magnetic resonance (NMR) spectroscopy titrations. In two-dimensional nuclear Overhauser enhancement spectroscopy experiments boxB RNA in complex with Nun-(20-44) exhibits the same pattern of resonances as it does in complex with N peptides containing the ARM, and we could show that Nun-(20-44) forms a bent alpha-helix upon binding to the boxB RNA. The structure of the boxB RNA-bound Nun-(20-44) was determined on the basis of 191 intra- and 30 intermolecular distance restraints. Ser-24 is anchored to the lower RNA stem, and stacking of Tyr-39 and A7 is clearly experimentally indicated. Arg-28 shows numerous contacts to the RNA stem. Leu-22, Ile-30, Trp-33, Ile-37, and Leu-41 form a hydrophobic surface, which could be a recognition site for additional host factors such as NusG. Such a hydrophobic surface area is not present in N-(1-36) bound to boxB RNA.
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==About this Structure==
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The structure of the coliphage HK022 Nun protein-lambda-phage boxB RNA complex. Implications for the mechanism of transcription termination.,Faber C, Scharpf M, Becker T, Sticht H, Rosch P J Biol Chem. 2001 Aug 24;276(34):32064-70. Epub 2001 May 16. PMID:11356847<ref>PMID:11356847</ref>
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1HJI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_hk022 Enterobacteria phage hk022]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HJI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structure of the coliphage HK022 Nun protein-lambda-phage boxB RNA complex. Implications for the mechanism of transcription termination., Faber C, Scharpf M, Becker T, Sticht H, Rosch P, J Biol Chem. 2001 Aug 24;276(34):32064-70. Epub 2001 May 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11356847 11356847]
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</div>
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[[Category: Enterobacteria phage hk022]]
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<div class="pdbe-citations 1hji" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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== References ==
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[[Category: Becker, T.]]
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<references/>
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[[Category: Faber, C.]]
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__TOC__
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[[Category: Roesch, P.]]
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</StructureSection>
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[[Category: Schaerpf, M.]]
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[[Category: Escherichia virus HK022]]
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[[Category: Sticht, H.]]
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[[Category: Escherichia virus Lambda]]
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[[Category: bacteriophage hk022]]
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[[Category: Large Structures]]
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[[Category: peptide-rna-complex]]
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[[Category: Becker T]]
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[[Category: peptide-rna-recognition]]
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[[Category: Faber C]]
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[[Category: protein/rna]]
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[[Category: Roesch P]]
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[[Category: termination]]
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[[Category: Schaerpf M]]
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[[Category: Sticht H]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:36:38 2007''
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BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX

PDB ID 1hji

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