6d30: Difference between revisions

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<StructureSection load='6d30' size='340' side='right' caption='[[6d30]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
<StructureSection load='6d30' size='340' side='right' caption='[[6d30]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6d30]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D30 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6d30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D30 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USB1, C16orf57 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6d30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d30 OCA], [http://pdbe.org/6d30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d30 RCSB], [http://www.ebi.ac.uk/pdbsum/6d30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d30 ProSAT]</span></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=6d30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d30 OCA], [http://pdbe.org/6d30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d30 RCSB], [http://www.ebi.ac.uk/pdbsum/6d30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d30 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/USB1_HUMAN USB1_HUMAN]] Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate.<ref>PMID:22899009</ref> <ref>PMID:23190533</ref>   
[[http://www.uniprot.org/uniprot/USB1_HUMAN USB1_HUMAN]] Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate.<ref>PMID:22899009</ref> <ref>PMID:23190533</ref>   
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Post-transcriptional modification of snRNA is central to spliceosome function. Usb1 is an exoribonuclease that shortens the oligo-uridine tail of U6 snRNA, resulting in a terminal 2',3' cyclic phosphate group in most eukaryotes, including humans. Loss of function mutations in human Usb1 cause the rare disorder poikiloderma with neutropenia (PN), and result in U6 snRNAs with elongated 3' ends that are aberrantly adenylated. Here, we show that human Usb1 removes 3' adenosines with 20-fold greater efficiency than uridines, which explains the presence of adenylated U6 snRNAs in cells lacking Usb1. We determined three high-resolution co-crystal structures of Usb1: wild-type Usb1 bound to the substrate analog adenosine 5'-monophosphate, and an inactive mutant bound to RNAs with a 3' terminal adenosine and uridine. These structures, along with QM/MM MD simulations of the catalytic mechanism, illuminate the molecular basis for preferential deadenylation of U6 snRNA. The extent of Usb1 processing is influenced by the secondary structure of U6 snRNA.
Structural and mechanistic basis for preferential deadenylation of U6 snRNA by Usb1.,Nomura Y, Roston D, Montemayor EJ, Cui Q, Butcher SE Nucleic Acids Res. 2018 Sep 12. pii: 5095463. doi: 10.1093/nar/gky812. PMID:30215753<ref>PMID:30215753</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6d30" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Butcher, S E]]
[[Category: Butcher, S E]]
[[Category: Montemayor, E J]]
[[Category: Montemayor, E J]]

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