3pie

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Current revision (10:41, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3pie' size='340' side='right'caption='[[3pie]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3pie' size='340' side='right'caption='[[3pie]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pie]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_56498 Atcc 56498]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pie]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIE FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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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]] 2.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pif|3pif]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0F22385g ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28985 ATCC 56498])</td></tr>
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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=3pie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pie OCA], [https://pdbe.org/3pie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pie RCSB], [https://www.ebi.ac.uk/pdbsum/3pie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pie 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=3pie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pie OCA], [https://pdbe.org/3pie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pie RCSB], [https://www.ebi.ac.uk/pdbsum/3pie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pie ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q6CJ09_KLULA Q6CJ09_KLULA]
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The 5'--&gt;3' exoribonucleases (XRNs) have important functions in transcription, RNA metabolism and RNA interference. The structure of Rat1 (also known as Xrn2) showed that the two highly conserved regions of XRNs form a single, large domain that defines the active site of the enzyme. Xrn1 has a 510-residue segment after the conserved regions that is required for activity but is absent from Rat1/Xrn2. Here we report the crystal structures of Kluyveromyces lactis Xrn1 (residues 1-1,245, E178Q mutant), alone and in complex with a Mn(2+) ion in the active site. The 510-residue segment contains four domains (D1-D4), located far from the active site. Our mutagenesis and biochemical studies show that their functional importance results from their ability to stabilize the conformation of the N-terminal segment of Xrn1. These domains might also constitute a platform that interacts with protein partners of Xrn1.
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Structural and biochemical studies of the 5'--&gt;3' exoribonuclease Xrn1.,Chang JH, Xiang S, Xiang K, Manley JL, Tong L Nat Struct Mol Biol. 2011 Mar;18(3):270-6. doi: 10.1038/nsmb.1984. Epub 2011 Feb , 6. PMID:21297639<ref>PMID:21297639</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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<div class="pdbe-citations 3pie" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 56498]]
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[[Category: Kluyveromyces lactis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chang, J H]]
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[[Category: Chang JH]]
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[[Category: Tong, L]]
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[[Category: Tong L]]
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[[Category: Xiang, S]]
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[[Category: Xiang S]]
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[[Category: Beta berrel]]
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[[Category: Chromo domain]]
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[[Category: Dna binding]]
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[[Category: Hydrolase]]
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[[Category: Mrna turnover]]
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[[Category: Rna binding]]
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[[Category: Rrna processing]]
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[[Category: Tudor domain]]
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Current revision

Crystal structure of the 5'->3' exoribonuclease Xrn1, E178Q mutant

PDB ID 3pie

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OCA

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