3kbl

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==Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans N169A mutant at 2.28 A resolution==
==Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans N169A mutant at 2.28 A resolution==
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<StructureSection load='3kbl' size='340' side='right' caption='[[3kbl]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
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<StructureSection load='3kbl' size='340' side='right'caption='[[3kbl]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3kbl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KBL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KBL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3kbl]] is a 4 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=3KBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KBL FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k6t|3k6t]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gld-1, T23G11.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbl OCA], [https://pdbe.org/3kbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kbl RCSB], [https://www.ebi.ac.uk/pdbsum/3kbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kbl ProSAT]</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=3kbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kbl RCSB], [http://www.ebi.ac.uk/pdbsum/3kbl PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GLD1_CAEEL GLD1_CAEEL]] Germ line-specific tumor suppressor essential for oogenesis. Controls the spatial pattern of translation of multiple oogenesis specific mRNAs (e.g. yolk receptor rme-2) by repression of translation during early meiotic prophase (leptotene to pachytene) and then derepression of translation during diplotene/ diakinesis, following its degradation. Also functions to promote the male sexual fate in the hermaphrodite germline but not the male germline. Functions redundantly with gld-2 to promote the initiation of meiotic development and/or inhibit stem cell proliferation.
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[https://www.uniprot.org/uniprot/GLD1_CAEEL GLD1_CAEEL] Germ line-specific tumor suppressor essential for oogenesis. Controls the spatial pattern of translation of multiple oogenesis specific mRNAs (e.g. yolk receptor rme-2) by repression of translation during early meiotic prophase (leptotene to pachytene) and then derepression of translation during diplotene/ diakinesis, following its degradation. Also functions to promote the male sexual fate in the hermaphrodite germline but not the male germline. Functions redundantly with gld-2 to promote the initiation of meiotic development and/or inhibit stem cell proliferation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/3kbl_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/3kbl_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=3kbl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Posttranscriptional regulation of gene expression is an important mechanism for modulating protein levels in eukaryotes, especially in developmental pathways. The highly conserved homodimeric STAR/GSG proteins play a key role in regulating translation by binding bipartite consensus sequences in the untranslated regions of target mRNAs, but the exact mechanism remains unknown. Structures of STAR protein RNA binding subdomains have been determined, but structural information is lacking for the homodimerization subdomain. Here, we present the structure of the C. elegans GLD-1 homodimerization domain dimer, determined by a combination of X-ray crystallography and NMR spectroscopy, revealing a helix-turn-helix monomeric fold with the two protomers stacked perpendicularly. Structure-based mutagenesis demonstrates that the dimer interface is not easily disrupted, but the structural integrity of the monomer is crucial for GLD-1 dimerization. Finally, an improved model for STAR-mediated translational regulation of mRNA, based on the GLD-1 homodimerization domain structure, is presented.
 
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Structure of the GLD-1 homodimerization domain: insights into STAR protein-mediated translational regulation.,Beuck C, Szymczyna BR, Kerkow DE, Carmel AB, Columbus L, Stanfield RL, Williamson JR Structure. 2010 Mar 10;18(3):377-89. PMID:20223220<ref>PMID:20223220</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Beuck, C]]
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[[Category: Large Structures]]
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[[Category: Carmel, A B]]
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[[Category: Beuck C]]
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[[Category: Columbus, L]]
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[[Category: Carmel AB]]
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[[Category: Kerkow, D E]]
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[[Category: Columbus L]]
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[[Category: Stanfield, R L]]
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[[Category: Kerkow DE]]
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[[Category: Szymczyna, B R]]
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[[Category: Stanfield RL]]
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[[Category: Williamson, J R]]
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[[Category: Szymczyna BR]]
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[[Category: Developmental protein]]
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[[Category: Williamson JR]]
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[[Category: Differentiation]]
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[[Category: Gld-1]]
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[[Category: Helix-turn-helix motif]]
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[[Category: Hydrophobic homodimer interface]]
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[[Category: Meiosis]]
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[[Category: N169a mutant]]
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[[Category: Oogenesis]]
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[[Category: Perpendicular stacking of protomer]]
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[[Category: Protein binding]]
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[[Category: Qua1 homodimerization domain]]
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[[Category: Rna-binding]]
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[[Category: Translation regulation]]
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Current revision

Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans N169A mutant at 2.28 A resolution

PDB ID 3kbl

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