3pie: Difference between revisions
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==Crystal structure of the 5'->3' exoribonuclease Xrn1, E178Q mutant== | |||
<StructureSection load='3pie' size='340' side='right' caption='[[3pie]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pie]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PIE FirstGlance]. <br> | |||
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pif|3pif]]</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 Kluyveromyces lactis])</td></tr> | |||
<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=3pie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pie OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pie RCSB], [http://www.ebi.ac.uk/pdbsum/3pie PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kluyveromyces lactis]] | [[Category: Kluyveromyces lactis]] | ||
[[Category: Chang, J H | [[Category: Chang, J H]] | ||
[[Category: Tong, L | [[Category: Tong, L]] | ||
[[Category: Xiang, S | [[Category: Xiang, S]] | ||
[[Category: Beta berrel]] | [[Category: Beta berrel]] | ||
[[Category: Chromo domain]] | [[Category: Chromo domain]] | ||
Revision as of 07:05, 19 December 2014
Crystal structure of the 5'->3' exoribonuclease Xrn1, E178Q mutant
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