1uoc

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{{Seed}}
 
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[[Image:1uoc.png|left|200px]]
 
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==X-ray structure of the RNase domain of the yeast Pop2 protein==
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The line below this paragraph, containing "STRUCTURE_1uoc", creates the "Structure Box" on the page.
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<StructureSection load='1uoc' size='340' side='right'caption='[[1uoc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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{{STRUCTURE_1uoc| PDB=1uoc | SCENE= }}
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uo/1uoc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1uoc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===X-RAY STRUCTURE OF THE RNASE DOMAIN OF THE YEAST POP2 PROTEIN===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14618157}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1uoc" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14618157 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14618157}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1UOC is a 2 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:14618157</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Mauxion, F.]]
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[[Category: Mauxion F]]
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[[Category: Seraphin, B.]]
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[[Category: Seraphin B]]
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[[Category: Suck, D.]]
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[[Category: Suck D]]
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[[Category: Thore, S.]]
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[[Category: Thore S]]
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[[Category: Dedd nuclease]]
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[[Category: Hydrolase]]
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[[Category: Mrna degradation]]
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[[Category: Phosphorylation.]]
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[[Category: Repressor]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:48:35 2009''
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Current revision

X-ray structure of the RNase domain of the yeast Pop2 protein

PDB ID 1uoc

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