5bym
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BYM FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BYM FirstGlance]. <br> | ||
| - | </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=5bym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bym OCA], [https://pdbe.org/5bym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bym RCSB], [https://www.ebi.ac.uk/pdbsum/5bym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bym 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]] 2.708Å</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=5bym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bym OCA], [https://pdbe.org/5bym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bym RCSB], [https://www.ebi.ac.uk/pdbsum/5bym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bym ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MPT5_YEAST MPT5_YEAST] RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of HO by binding to the 3'-UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin modifiers and spindle pole body components. Recognizes and binds to 5'-TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor of POP2 mutation. Required for high temperature growth.<ref>PMID:11157761</ref> | [https://www.uniprot.org/uniprot/MPT5_YEAST MPT5_YEAST] RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of HO by binding to the 3'-UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin modifiers and spindle pole body components. Recognizes and binds to 5'-TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor of POP2 mutation. Required for high temperature growth.<ref>PMID:11157761</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Proteins bind and control mRNAs, directing their localization, translation and stability. Members of the PUF family of RNA-binding proteins control multiple mRNAs in a single cell, and play key roles in development, stem cell maintenance and memory formation. Here we identified the mRNA targets of a S. cerevisiae PUF protein, Puf5p, by ultraviolet-crosslinking-affinity purification and high-throughput sequencing (HITS-CLIP). The binding sites recognized by Puf5p are diverse, with variable spacer lengths between two specific sequences. Each length of site correlates with a distinct biological function. Crystal structures of Puf5p-RNA complexes reveal that the protein scaffold presents an exceptionally flat and extended interaction surface relative to other PUF proteins. In complexes with RNAs of different lengths, the protein is unchanged. A single PUF protein repeat is sufficient to induce broadening of specificity. Changes in protein architecture, such as alterations in curvature, may lead to evolution of mRNA regulatory networks. | ||
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| - | RNA regulatory networks diversified through curvature of the PUF protein scaffold.,Wilinski D, Qiu C, Lapointe CP, Nevil M, Campbell ZT, Tanaka Hall TM, Wickens M Nat Commun. 2015 Sep 14;6:8213. doi: 10.1038/ncomms9213. PMID:26364903<ref>PMID:26364903</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5bym" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of the RNA-binding domain of yeast Puf5p bound to SMX2 RNA
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