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| | ==Structural Characterization of Nop10p using Nuclear Magnetic Resonance Spectroscopy== | | ==Structural Characterization of Nop10p using Nuclear Magnetic Resonance Spectroscopy== |
| - | <StructureSection load='1y2y' size='340' side='right'caption='[[1y2y]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1y2y' size='340' side='right'caption='[[1y2y]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y2y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y2Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y2y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y2Y FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NOP10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | </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'>[http://proteopedia.org/fgij/fg.htm?mol=1y2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2y OCA], [http://pdbe.org/1y2y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y2y RCSB], [http://www.ebi.ac.uk/pdbsum/1y2y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y2y 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=1y2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2y OCA], [https://pdbe.org/1y2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y2y RCSB], [https://www.ebi.ac.uk/pdbsum/1y2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y2y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NOP10_YEAST NOP10_YEAST]] Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs. Essential for growth.<ref>PMID:9843512</ref> | + | [https://www.uniprot.org/uniprot/NOP10_YEAST NOP10_YEAST] Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs. Essential for growth.<ref>PMID:9843512</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Ribosome biogenesis protein|Ribosome biogenesis protein]] | + | *[[Ribosome biogenesis protein 3D structures|Ribosome biogenesis protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Caizergues-Ferrer, M]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Feigon, J]] | + | [[Category: Caizergues-Ferrer M]] |
| - | [[Category: Johansson, C]] | + | [[Category: Feigon J]] |
| - | [[Category: Khanna, M]] | + | [[Category: Johansson C]] |
| - | [[Category: Wu, H]] | + | [[Category: Khanna M]] |
| - | [[Category: Biosynthetic protein]]
| + | [[Category: Wu H]] |
| - | [[Category: Box h/aca snorna]]
| + | |
| - | [[Category: Pseudouridine]]
| + | |
| - | [[Category: Snornp]]
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| Structural highlights
Function
NOP10_YEAST Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs. Essential for growth.[1]
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 H/ACA small nucleolar ribonucleoprotein (snoRNP) complexes guide the modification of uridine to pseudouridine at conserved sites in rRNA. The H/ACA snoRNPs each comprise a target-site-specific snoRNA and four core proteins, Nop10p, Nhp2p, Gar1p, and the pseudouridine synthase, Cbf5p, in yeast. The secondary structure of the H/ACA snoRNAs includes two hairpins that each contain a large internal loop (the pseudouridylation pocket), one or both of which are partially complementary to the target RNA(s). We have determined the solution structure of an RNA hairpin derived from the human U65 box H/ACA snoRNA including the pseudouridylation pocket and adjacent stems, providing the first three-dimensional structural information on these H/ACA snoRNAs. We have also determined the structure of Nop10p and investigated its interaction with RNA using NMR spectroscopy. Nop10p contains a structurally well-defined N-terminal region composed of a beta-hairpin, and the rest of the protein lacks a globular structure. Chemical shift mapping of the interaction of RNA constructs of U65 box H/ACA 3' hairpin with Nop10p shows that the beta-hairpin binds weakly but specifically to RNA. The unstructured region of Nop10p likely interacts with Cbf5p.
Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA.,Khanna M, Wu H, Johansson C, Caizergues-Ferrer M, Feigon J RNA. 2006 Jan;12(1):40-52. PMID:16373493[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Henras A, Henry Y, Bousquet-Antonelli C, Noaillac-Depeyre J, Gelugne JP, Caizergues-Ferrer M. Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs. EMBO J. 1998 Dec 1;17(23):7078-90. PMID:9843512 doi:10.1093/emboj/17.23.7078
- ↑ Khanna M, Wu H, Johansson C, Caizergues-Ferrer M, Feigon J. Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA. RNA. 2006 Jan;12(1):40-52. PMID:16373493 doi:12/1/40
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