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1uoc
From Proteopedia
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| - | [[Image:1uoc.gif|left|200px]]<br /><applet load="1uoc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1uoc, resolution 2.30Å" /> | ||
| - | '''X-RAY STRUCTURE OF THE RNASE DOMAIN OF THE YEAST POP2 PROTEIN'''<br /> | ||
| - | == | + | ==X-ray structure of the RNase domain of the yeast Pop2 protein== |
| - | In Saccharomyces cerevisiae, a large complex, known as the Ccr4-Not | + | <StructureSection load='1uoc' size='340' side='right'caption='[[1uoc]], [[Resolution|resolution]] 2.30Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1uoc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UOC FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></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=1uoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uoc OCA], [https://pdbe.org/1uoc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uoc RCSB], [https://www.ebi.ac.uk/pdbsum/1uoc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uoc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/POP2_YEAST POP2_YEAST] Acts as probably catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vitro, POP2 has 3'-exoribonuclease activity with a preference for poly(A) RNAs, but also degrades poly(U) and poly(C) RNAs. Is part of a glucose-sensing system involved in growth control in response to glucose availability.<ref>PMID:9463387</ref> <ref>PMID:11239395</ref> <ref>PMID:11410650</ref> <ref>PMID:14618157</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uo/1uoc_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1uoc ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In Saccharomyces cerevisiae, a large complex, known as the Ccr4-Not complex, containing two nucleases, is responsible for mRNA deadenylation. One of these nucleases is called Pop2 and has been identified by similarity with PARN, a human poly(A) nuclease. Here, we present the crystal structure of the nuclease domain of Pop2 at 2.3 A resolution. The domain has the fold of the DnaQ family and represents the first structure of an RNase from the DEDD superfamily. Despite the presence of two non-canonical residues in the active site, the domain displays RNase activity on a broad range of RNA substrates. Site-directed mutagenesis of active-site residues demonstrates the intrinsic ability of the Pop2 RNase D domain to digest RNA. This first structure of a nuclease involved in the 3'-5' deadenylation of mRNA in yeast provides information for the understanding of the mechanism by which the Ccr4-Not complex achieves its functions. | ||
| - | + | X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex.,Thore S, Mauxion F, Seraphin B, Suck D EMBO Rep. 2003 Dec;4(12):1150-5. Epub 2003 Nov 14. PMID:14618157<ref>PMID:14618157</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1uoc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | + | [[Category: Mauxion F]] | |
| - | [[Category: Mauxion | + | [[Category: Seraphin B]] |
| - | [[Category: Seraphin | + | [[Category: Suck D]] |
| - | [[Category: Suck | + | [[Category: Thore S]] |
| - | [[Category: Thore | + | |
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Current revision
X-ray structure of the RNase domain of the yeast Pop2 protein
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