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| | ==Structure of a C.elegans sex determining protein== | | ==Structure of a C.elegans sex determining protein== |
| - | <StructureSection load='4jnd' size='340' side='right' caption='[[4jnd]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='4jnd' size='340' side='right'caption='[[4jnd]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jnd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. 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 [http://oca.weizmann.ac.il/oca-docs/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"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fem-2, T19C3.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnd OCA], [http://pdbe.org/4jnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jnd RCSB], [http://www.ebi.ac.uk/pdbsum/4jnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Phosphoprotein phosphatase]] | + | [[Category: Large Structures]] |
| - | [[Category: Feng, Y]] | + | [[Category: Feng Y]] |
| - | [[Category: Ge, J]] | + | [[Category: Ge J]] |
| - | [[Category: Yang, M]] | + | [[Category: Yang M]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Zhang Y]] |
| - | [[Category: Cytosol]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Male promoting]]
| + | |
| - | [[Category: Novel fold]]
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| - | [[Category: Sex determination]]
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| Structural highlights
Function
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.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Y, Zhao H, Wang J, Ge J, Li Y, Gu J, Li P, Feng Y, Yang M. Structural insight into Caenorhabditis elegans sex-determining protein FEM-2. J Biol Chem. 2013 Jul 26;288(30):22058-66. doi: 10.1074/jbc.M113.464339. Epub, 2013 Jun 11. PMID:23760267 doi:http://dx.doi.org/10.1074/jbc.M113.464339
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