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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/Atcc_43587 Atcc 43587]. 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> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flpA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr> | + | </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/FLPA_PYRFU FLPA_PYRFU]] Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity).[HAMAP-Rule:MF_00351]
| + | [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: Atcc 43587]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, H]] | + | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Oruganti, S]] | + | [[Category: Li H]] |
| - | [[Category: Terns, M P]] | + | [[Category: Oruganti S]] |
| - | [[Category: Terns, R]] | + | [[Category: Terns MP]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Terns R]] |
| - | [[Category: Box c/d]]
| + | [[Category: Zhang Y]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q8U4M1_PYRFU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The 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
- ↑ Oruganti S, Zhang Y, Li H, Robinson H, Terns MP, Terns RM, Yang W, Li H. Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. J Mol Biol. 2007 Aug 31;371(5):1141-50. Epub 2007 Jun 15. PMID:17617422 doi:10.1016/j.jmb.2007.06.029
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