|
|
Line 3: |
Line 3: |
| <StructureSection load='1i5l' size='340' side='right'caption='[[1i5l]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='1i5l' size='340' side='right'caption='[[1i5l]], [[Resolution|resolution]] 2.75Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1i5l]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1I5L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1i5l]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5L FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=URI:URIDINE'>URI</scene></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]] 2.75Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d3b|1d3b]], [[1b34|1b34]], [[1i4k|1i4k]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=URI:URIDINE'>URI</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF0875 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</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=1i5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5l OCA], [https://pdbe.org/1i5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5l RCSB], [https://www.ebi.ac.uk/pdbsum/1i5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5l ProSAT]</span></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=1i5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5l OCA], [http://pdbe.org/1i5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i5l RCSB], [http://www.ebi.ac.uk/pdbsum/1i5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5l ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/RUXX_ARCFU RUXX_ARCFU] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
Line 30: |
Line 31: |
| | | |
| ==See Also== | | ==See Also== |
- | *[[Sm-like protein|Sm-like protein]] | + | *[[Sm-like protein 3D structures|Sm-like protein 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Arcfl]] | + | [[Category: Archaeoglobus fulgidus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Basquin, J]] | + | [[Category: Basquin J]] |
- | [[Category: Mayer, C]] | + | [[Category: Mayer C]] |
- | [[Category: Seraphin, B]] | + | [[Category: Seraphin B]] |
- | [[Category: Suck, D]] | + | [[Category: Suck D]] |
- | [[Category: Thore, S]] | + | [[Category: Thore S]] |
- | [[Category: Toro, I]] | + | [[Category: Toro I]] |
- | [[Category: Core snrnp domain]]
| + | |
- | [[Category: Rna binding protein]]
| + | |
- | [[Category: Rna binding protein-rna complex]]
| + | |
- | [[Category: Single-stranded rna binding protein]]
| + | |
- | [[Category: Sm]]
| + | |
- | [[Category: Snrnp]]
| + | |
| Structural highlights
Function
RUXX_ARCFU
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
Eukaryotic Sm and Sm-like proteins associate with RNA to form the core domain of ribonucleoprotein particles involved in pre-mRNA splicing and other processes. Recently, putative Sm proteins of unknown function have been identified in ARCHAEA: We show by immunoprecipitation experiments that the two Sm proteins present in Archaeoglobus fulgidus (AF-Sm1 and AF-Sm2) associate with RNase P RNA in vivo, suggesting a role in tRNA processing. The AF-Sm1 protein also interacts specifically with oligouridylate in vitro. We have solved the crystal structures of this protein and a complex with RNA. AF-Sm1 forms a seven-membered ring, with the RNA interacting inside the central cavity on one face of the doughnut-shaped complex. The bases are bound via stacking and specific hydrogen bonding contacts in pockets lined by residues highly conserved in archaeal and eukaryotic Sm proteins, while the phosphates remain solvent accessible. A comparison with the structures of human Sm protein dimers reveals closely related monomer folds and intersubunit contacts, indicating that the architecture of the Sm core domain and RNA binding have been conserved during evolution.
RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.,Toro I, Thore S, Mayer C, Basquin J, Seraphin B, Suck D EMBO J. 2001 May 1;20(9):2293-303. PMID:11331594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Toro I, Thore S, Mayer C, Basquin J, Seraphin B, Suck D. RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex. EMBO J. 2001 May 1;20(9):2293-303. PMID:11331594 doi:10.1093/emboj/20.9.2293
|