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==BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX== | |||
<StructureSection load='1hji' size='340' side='right'caption='[[1hji]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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=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> | |||
</table> | |||
== Function == | |||
''' | [https://www.uniprot.org/uniprot/VNUN_BPHK0 VNUN_BPHK0] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
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. | 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. | ||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1hji" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Becker | <references/> | ||
[[Category: Faber | __TOC__ | ||
[[Category: Roesch | </StructureSection> | ||
[[Category: Schaerpf | [[Category: Escherichia virus HK022]] | ||
[[Category: Sticht | [[Category: Escherichia virus Lambda]] | ||
[[Category: Large Structures]] | |||
[[Category: Becker T]] | |||
[[Category: Faber C]] | |||
[[Category: Roesch P]] | |||
[[Category: Schaerpf M]] | |||
[[Category: Sticht H]] | |||
Latest revision as of 08:31, 15 May 2024
BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEXBACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX
Structural highlights
FunctionPublication Abstract from PubMedNun 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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