4jnd
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jnd]] is a 1 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=4JND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JND FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jnd]] is a 1 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=4JND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JND FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.652Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4jnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnd OCA], [https://pdbe.org/4jnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jnd RCSB], [https://www.ebi.ac.uk/pdbsum/4jnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnd ProSAT]</span></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=4jnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnd OCA], [https://pdbe.org/4jnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jnd RCSB], [https://www.ebi.ac.uk/pdbsum/4jnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FEM2_CAEEL FEM2_CAEEL] Probable phosphatase involved in the regulation of sex determination. Plays an important role in regulating a pathway transducing a non-cell-autonomous signal to a nuclear transcription factor. Promotes apoptosis. Together with fem-3 associates with the CBC(fem-1) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of tra-1. | [https://www.uniprot.org/uniprot/FEM2_CAEEL FEM2_CAEEL] Probable phosphatase involved in the regulation of sex determination. Plays an important role in regulating a pathway transducing a non-cell-autonomous signal to a nuclear transcription factor. Promotes apoptosis. Together with fem-3 associates with the CBC(fem-1) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of tra-1. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | In the nematode Caenorhabditis elegans, fem-1, fem-2, and fem-3 play crucial roles in male sexual development. Among these three genes, fem-2 encodes a PP2C (serine/threonine phosphatase type 2C)-like protein, whose activity promotes the development of masculinity. Different from the canonical PP2Cs, FEM-2 consists of an additional N-terminal domain (NTD) apart from its C-terminal catalytic domain. Interestingly, genetic studies have indicated indispensable roles for both of these two domains of FEM-2 in promoting male development, but the underlying mechanism remains unknown. In the present study, we solved the crystal structure of full-length FEM-2, which revealed a novel structural fold formed by its NTD. Structural and functional analyses demonstrated that the NTD did not directly regulate the in vitro dephosphorylation activity of FEM-2, but instead functioned as a scaffold domain in the assembly of the FEM-1/2/3 complex, the executioner in the final step of the sex determination pathway. Biochemical studies further identified the regions in the NTD involved in FEM-1 and FEM-3 interactions. Our results not only identified a novel fold formed by the extra domain of a noncanonical PP2C enzyme, but also provided important insights into the molecular mechanism of how the NTD works in mediating the sex-determining role of FEM-1/2/3 complex. | ||
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| - | Structural insight into Caenorhabditis elegans sex-determining protein FEM-2.,Zhang Y, Zhao H, Wang J, Ge J, Li Y, Gu J, Li P, Feng Y, Yang M J Biol Chem. 2013 Jul 26;288(30):22058-66. doi: 10.1074/jbc.M113.464339. Epub, 2013 Jun 11. PMID:23760267<ref>PMID:23760267</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4jnd" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of a C.elegans sex determining protein
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