5o20: Difference between revisions

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==Structure of Nrd1 RNA binding domain in complex with RNA (UUAGUAAUCC)==
==Structure of Nrd1 RNA binding domain in complex with RNA (UUAGUAAUCC)==
<StructureSection load='5o20' size='340' side='right' caption='[[5o20]], [[Resolution|resolution]] 3.53&Aring;' scene=''>
<StructureSection load='5o20' size='340' side='right'caption='[[5o20]], [[Resolution|resolution]] 3.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5o20]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O20 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O20 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5o20]] 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=5O20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O20 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 3.53&#8491;</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=5o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o20 OCA], [http://pdbe.org/5o20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o20 RCSB], [http://www.ebi.ac.uk/pdbsum/5o20 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o20 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=5o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o20 OCA], [https://pdbe.org/5o20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o20 RCSB], [https://www.ebi.ac.uk/pdbsum/5o20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o20 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NRD1_YEAST NRD1_YEAST]] Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.  
[https://www.uniprot.org/uniprot/NRD1_YEAST NRD1_YEAST] Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transcription termination of non-coding RNAs is regulated in yeast by a complex of three RNA binding proteins: Nrd1, Nab3 and Sen1. Nrd1 is central in this process by interacting with Rbp1 of RNA polymerase II, Trf4 of TRAMP and GUAA/G terminator sequences. We lack structural data for the last of these binding events. We determined the structures of Nrd1 RNA binding domain and its complexes with three GUAA-containing RNAs, characterized RNA binding energetics and tested rationally designed mutants in vivo. The Nrd1 structure shows an RRM domain fused with a second alpha/beta domain that we name split domain (SD), because it is formed by two non-consecutive segments at each side of the RRM. The GUAA interacts with both domains and with a pocket of water molecules, trapped between the two stacking adenines and the SD. Comprehensive binding studies demonstrate for the first time that Nrd1 has a slight preference for GUAA over GUAG and genetic and functional studies suggest that Nrd1 RNA binding domain might play further roles in non-coding RNAs transcription termination.
 
The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.,Franco-Echevarria E, Gonzalez-Polo N, Zorrilla S, Martinez-Lumbreras S, Santiveri CM, Campos-Olivas R, Sanchez M, Calvo O, Gonzalez B, Perez-Canadillas JM Nucleic Acids Res. 2017 Sep 29;45(17):10293-10305. doi: 10.1093/nar/gkx685. PMID:28973465<ref>PMID:28973465</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5o20" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Franco-Echevarria, E]]
[[Category: Large Structures]]
[[Category: Gonzalez, B]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Perez-Canadillas, J M]]
[[Category: Franco-Echevarria E]]
[[Category: Nrd1]]
[[Category: Gonzalez B]]
[[Category: Nrd1 complex]]
[[Category: Perez-Canadillas JM]]
[[Category: Rna-binding]]
[[Category: Rrm]]
[[Category: Transcription]]
[[Category: Transcription non-coding rna]]
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