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| | <StructureSection load='5o1z' size='340' side='right'caption='[[5o1z]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='5o1z' size='340' side='right'caption='[[5o1z]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5o1z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O1Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O1Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5o1z]] 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=5O1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O1Z FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5o1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1z OCA], [http://pdbe.org/5o1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o1z RCSB], [http://www.ebi.ac.uk/pdbsum/5o1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1z ProSAT]</span></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]] 3.4Å</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=5o1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1z OCA], [https://pdbe.org/5o1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o1z RCSB], [https://www.ebi.ac.uk/pdbsum/5o1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1z 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Franco-Echevarria, E]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Gonzalez, B]] | + | [[Category: Franco-Echevarria E]] |
| - | [[Category: Perez-Canadillas, J M]] | + | [[Category: Gonzalez B]] |
| - | [[Category: Nrd1]]
| + | [[Category: Perez-Canadillas JM]] |
| - | [[Category: Nrd1 complex]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Rrm]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription non-coding rna]]
| + | |
| Structural highlights
Function
NRD1_YEAST Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition. Nucleic Acids Res. 2017 Sep 29;45(17):10293-10305. doi: 10.1093/nar/gkx685. PMID:28973465 doi:http://dx.doi.org/10.1093/nar/gkx685
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