2nnw: Difference between revisions
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<StructureSection load='2nnw' size='340' side='right'caption='[[2nnw]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2nnw' size='340' side='right'caption='[[2nnw]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nnw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2nnw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNW FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=2nnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnw OCA], [https://pdbe.org/2nnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnw RCSB], [https://www.ebi.ac.uk/pdbsum/2nnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnw ProSAT]</span></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=2nnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnw OCA], [https://pdbe.org/2nnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnw RCSB], [https://www.ebi.ac.uk/pdbsum/2nnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q8U4M1_PYRFU Q8U4M1_PYRFU] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li | [[Category: Pyrococcus furiosus]] | ||
[[Category: Oruganti | [[Category: Li H]] | ||
[[Category: Terns | [[Category: Oruganti S]] | ||
[[Category: Terns | [[Category: Terns MP]] | ||
[[Category: Zhang | [[Category: Terns R]] | ||
[[Category: Zhang Y]] | |||
Latest revision as of 03:09, 28 December 2023
Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPsAlternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Nop56/58-fibrillarin heterocomplex is a core protein complex of the box C/D ribonucleoprotein particles that modify and process ribosomal RNAs. The previous crystal structure of the Archaeoglobus fulgidus complex revealed a symmetric dimer of two Nop56/58-fibrillarin complexes linked by the coiled-coil domains of the Nop56/68 proteins. However, because the A. fulgidus Nop56/58 protein lacks some domains found in most other species, it was thought that the bipartite architecture of the heterocomplex was not likely a general phenomenon. Here we report the crystal structure of the Nop56/58-fibrillarin complex bound with methylation cofactor, S-adenosyl-L-methionine from Pyrococcus furiosus, at 2.7 A. The new complex confirms the generality of the previously observed bipartite arrangement. In addition however, the conformation of Nop56/58 in the new structure differs substantially from that in the earlier structure. The distinct conformations of Nop56/58 suggest potential flexibility in Nop56/58. Computational normal mode analysis supports this view. Importantly, fibrillarin is repositioned within the two complexes. We propose that hinge motion within Nop56/58 has important implications for the possibility of simultaneously positioning two catalytic sites at the two target sites of a bipartite box C/D guide RNA. Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs.,Oruganti S, Zhang Y, Li H, Robinson H, Terns MP, Terns RM, Yang W, Li H J Mol Biol. 2007 Aug 31;371(5):1141-50. Epub 2007 Jun 15. PMID:17617422[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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