1hji: Difference between revisions

Revision as of 14:02, 21 February 2008

BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX

OverviewOverview

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.

About this StructureAbout this Structure

1HJI is a Protein complex structure of sequences from Enterobacteria phage hk022. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:01:57 2008

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OCA

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 '''BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX'''<br />
 ==Overview==
-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.
 ==About this Structure==
-HJI 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].
+HJI 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJI OCA].
 ==Reference==
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