1i4k: Difference between revisions

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<StructureSection load='1i4k' size='340' side='right'caption='[[1i4k]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1i4k' size='340' side='right'caption='[[1i4k]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1i4k]] is a 28 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=1I4K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1I4K FirstGlance]. <br>
<table><tr><td colspan='2'>[[1i4k]] is a 28 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=1I4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I4K FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d3b|1d3b]], [[1b34|1b34]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=1i4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4k OCA], [https://pdbe.org/1i4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i4k RCSB], [https://www.ebi.ac.uk/pdbsum/1i4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i4k 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=1i4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4k OCA], [http://pdbe.org/1i4k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i4k RCSB], [http://www.ebi.ac.uk/pdbsum/1i4k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i4k 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]]
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</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/main_output.php?pdb_ID=1i4k ConSurf].
</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/main_output.php?pdb_ID=1i4k ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:11331594</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i4k" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[AF-Sm1|AF-Sm1]]
*[[AF-Sm1|AF-Sm1]]
*[[Sm-like protein|Sm-like protein]]
*[[Sm-like protein 3D structures|Sm-like protein 3D structures]]
== 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: Sm]]
[[Category: Snrnp]]
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