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7s02
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Crystal structure of FBF-2 in complex with LST-1 site A peptide and FBE RNA== |
| - | <StructureSection load='7s02' size='340' side='right'caption='[[7s02]]' scene=''> | + | <StructureSection load='7s02' size='340' side='right'caption='[[7s02]], [[Resolution|resolution]] 2.34Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7s02]] is a 3 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=7S02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S02 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=7s02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s02 OCA], [https://pdbe.org/7s02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s02 RCSB], [https://www.ebi.ac.uk/pdbsum/7s02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s02 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]] 2.34Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7s02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s02 OCA], [https://pdbe.org/7s02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s02 RCSB], [https://www.ebi.ac.uk/pdbsum/7s02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s02 ProSAT]</span></td></tr> | ||
</table> | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In C. elegans, PUF proteins promote germline stem cell self-renewal. Their functions hinge on partnerships with two proteins that are redundantly required for stem cell maintenance. Here we focus on understanding how the essential partner protein, LST-1, modulates mRNA regulation by the PUF protein, FBF-2. LST-1 contains two nonidentical sites of interaction with FBF-2, LST-1 A and B. Our crystal structures of complexes of FBF-2, LST-1 A, and RNA visualize how FBF-2 associates with LST-1 A versus LST-1 B. One commonality is that FBF-2 contacts the conserved lysine and leucine side chains in the KxxL motifs in LST-1 A and B. A key difference is that FBF-2 forms unique contacts with regions N- and C-terminal to the KxxL motif. Consequently, LST-1 A does not modulate the RNA-binding affinity of FBF-2, whereas LST-1 B decreases RNA-binding affinity of FBF-2. The N-terminal region of LST-1 B, which binds near the 5' end of RNA elements, is essential to modulate FBF-2 RNA-binding affinity, while the C-terminal residues of LST-1 B contribute strong binding affinity to FBF-2. We conclude that LST-1 has the potential to impact which mRNAs are regulated depending on the precise nature of engagement through its functionally distinct FBF binding sites. | ||
| + | |||
| + | Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal.,Qiu C, Wine RN, Campbell ZT, Hall TMT Nucleic Acids Res. 2022 Jan 11;50(1):536-548. doi: 10.1093/nar/gkab1220. PMID:34908132<ref>PMID:34908132</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7s02" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Caenorhabditis elegans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Hall TMT]] |
| + | [[Category: Qiu C]] | ||
Current revision
Crystal structure of FBF-2 in complex with LST-1 site A peptide and FBE RNA
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