2iz8: Difference between revisions
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[[Image: | ==MS2-RNA HAIRPIN (C-7) COMPLEX== | ||
<StructureSection load='2iz8' size='340' side='right' caption='[[2iz8]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2iz8]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio phage ms2]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gkv 1gkv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IZ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IZ8 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aq3|1aq3]], [[1aq4|1aq4]], [[1bms|1bms]], [[1msc|1msc]], [[1mst|1mst]], [[1mva|1mva]], [[1mvb|1mvb]], [[1u1y|1u1y]], [[1zdh|1zdh]], [[1zdi|1zdi]], [[1zdj|1zdj]], [[1zdk|1zdk]], [[1zse|1zse]], [[2b2d|2b2d]], [[2b2e|2b2e]], [[2b2g|2b2g]], [[2bny|2bny]], [[2bq5|2bq5]], [[2bs0|2bs0]], [[2bs1|2bs1]], [[2bu1|2bu1]], [[2c4q|2c4q]], [[2c4y|2c4y]], [[2c4z|2c4z]], [[2c50|2c50]], [[2c51|2c51]], [[2ms2|2ms2]], [[5msf|5msf]], [[6msf|6msf]], [[7msf|7msf]], [[2iz9|2iz9]], [[2izm|2izm]], [[2izn|2izn]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iz8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iz8 RCSB], [http://www.ebi.ac.uk/pdbsum/2iz8 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iz/2iz8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have determined the structures of complexes between the phage MS2 coat protein and variants of the replicase translational operator in order to explore the sequence specificity of the RNA-protein interaction. The 19-nt RNA hairpins studied have substitutions at two positions that have been shown to be important for specific binding. At one of these positions, -10, which is a bulged adenosine (A) in the stem of the wild-type operator hairpin, substitutions were made with guanosine (G), cytidine (C) and two non-native bases, 2-aminopurine (2AP) and inosine (I). At the other position, -7 in the hairpin loop, the native adenine was substituted with a cytidine. Of these, only the G-10, C-10 and C-7 variants showed interpretable density for the RNA hairpin. In spite of large differences in binding affinities, the structures of the variant complexes are very similar to the wild-type operator complex. For G-10 substitutions in hairpin variants that can form bulges at alternative places in the stem, the binding affinity is low and a partly disordered conformation is seen in the electron density maps. The affinity is similar to that of wild-type when the base pairs adjacent to the bulged nucleotide are selected to avoid alternative conformations. Both purines bind in a very similar way in a pocket in the protein. In the C-10 variant, which has very low affinity, the cytidine is partly inserted in the protein pocket rather than intercalated in the RNA stem. Substitution of the wild-type adenosine at position -7 by pyrimidines gives strongly reduced affinities, but the structure of the C-7 complex shows that the base occupies the same position as the A-7 in the wild-type RNA. It is stacked in the RNA and makes no direct contact with the protein. | |||
Investigating the structural basis of purine specificity in the structures of MS2 coat protein RNA translational operator hairpins.,Helgstrand C, Grahn E, Moss T, Stonehouse NJ, Tars K, Stockley PG, Liljas L Nucleic Acids Res. 2002 Jun 15;30(12):2678-85. PMID:12060685<ref>PMID:12060685</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Enterobacterio phage ms2]] | [[Category: Enterobacterio phage ms2]] | ||
[[Category: Grahn, E.]] | [[Category: Grahn, E.]] |