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| | ==Crystal structure of the 5'->3' exoribonuclease Xrn1, E178Q mutant in Complex with Manganese== | | ==Crystal structure of the 5'->3' exoribonuclease Xrn1, E178Q mutant in Complex with Manganese== |
| - | <StructureSection load='3pif' size='340' side='right' caption='[[3pif]], [[Resolution|resolution]] 2.92Å' scene=''> | + | <StructureSection load='3pif' size='340' side='right'caption='[[3pif]], [[Resolution|resolution]] 2.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pif]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PIF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pif]] 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=3PIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.92Å</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>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pie|3pie]]</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=3pif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pif OCA], [https://pdbe.org/3pif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pif RCSB], [https://www.ebi.ac.uk/pdbsum/3pif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pif ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0F22385g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28985 Candida sphaerica])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pif OCA], [http://pdbe.org/3pif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pif RCSB], [http://www.ebi.ac.uk/pdbsum/3pif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pif ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q6CJ09_KLULA Q6CJ09_KLULA] |
| - | The 5'-->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'-->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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3pif" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candida sphaerica]] | + | [[Category: Kluyveromyces lactis]] |
| - | [[Category: Chang, J H]] | + | [[Category: Large Structures]] |
| - | [[Category: Tong, L]] | + | [[Category: Chang JH]] |
| - | [[Category: Xiang, S]] | + | [[Category: Tong L]] |
| - | [[Category: Beta berrel]] | + | [[Category: Xiang S]] |
| - | [[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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