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3k64
From Proteopedia
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| - | {{STRUCTURE_3k64| PDB=3k64 | SCENE= }} | ||
| - | ===Crystal structure of FBF-2/fem-3 PME complex=== | ||
| - | {{ABSTRACT_PUBMED_19901328}} | ||
| - | == | + | ==Crystal structure of FBF-2/fem-3 PME complex== |
| - | [[http://www.uniprot.org/uniprot/FBF2_CAEEL FBF2_CAEEL | + | <StructureSection load='3k64' size='340' side='right'caption='[[3k64]], [[Resolution|resolution]] 2.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3k64]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K64 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=3k64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k64 OCA], [https://pdbe.org/3k64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k64 RCSB], [https://www.ebi.ac.uk/pdbsum/3k64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k64 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FBF2_CAEEL FBF2_CAEEL] Involved in the control of stem cells and sex determination in the C.elegans hermaphrodite germline. May also play a role in the hermaphrodite germline proliferation and oogenesis. Binds specifically to the regulatory region of fem-3 3'-UTR and mediates the sperm/oocyte switch. Negatively regulates gld-3 expression possibly by directly binding to two sites within the gld-3 isoform B 3'-UTR.<ref>PMID:9393998</ref> <ref>PMID:15454534</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k64_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k64 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Caenorhabditis elegans fem-3 binding factor (FBF) is a founding member of the PUMILIO/FBF (PUF) family of mRNA regulatory proteins. It regulates multiple mRNAs critical for stem cell maintenance and germline development. Here, we report crystal structures of FBF in complex with 6 different 9-nt RNA sequences, including elements from 4 natural mRNAs. These structures reveal that FBF binds to conserved bases at positions 1-3 and 7-8. The key specificity determinant of FBF vs. other PUF proteins lies in positions 4-6. In FBF/RNA complexes, these bases stack directly with one another and turn away from the RNA-binding surface. A short region of FBF is sufficient to impart its unique specificity and lies directly opposite the flipped bases. We suggest that this region imposes a flattened curvature on the protein; hence, the requirement for the additional nucleotide. The principles of FBF/RNA recognition suggest a general mechanism by which PUF proteins recognize distinct families of RNAs yet exploit very nearly identical atomic contacts in doing so. | ||
| - | + | Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein.,Wang Y, Opperman L, Wickens M, Hall TM Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20186-91. Epub 2009 Nov 9. PMID:19901328<ref>PMID:19901328</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 3k64" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
| - | [[Category: Hall | + | [[Category: Large Structures]] |
| - | [[Category: Opperman | + | [[Category: Hall TMT]] |
| - | [[Category: Wang | + | [[Category: Opperman L]] |
| - | [[Category: Wickens | + | [[Category: Wang Y]] |
| - | + | [[Category: Wickens M]] | |
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Current revision
Crystal structure of FBF-2/fem-3 PME complex
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