3k6t

From Proteopedia

(Difference between revisions)

Revision as of 08:27, 1 November 2017

Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans at 2.04 A resolution

Structural highlights

3k6t is a 4 chain structure with sequence from Caeel. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	gld-1, T23G11.3 (CAEEL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Beuck C, Szymczyna BR, Kerkow DE, Carmel AB, Columbus L, Stanfield RL, Williamson JR. Structure of the GLD-1 homodimerization domain: insights into STAR protein-mediated translational regulation. Structure. 2010 Mar 10;18(3):377-89. PMID:20223220 doi:10.1016/j.str.2009.12.016

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3k6t"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans at 2.04 A resolution==
 <StructureSection load='3k6t' size='340' side='right' caption='[[3k6t]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[3k6t]] is a 4 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=3K6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K6T FirstGlance]. <br>
 </td></tr><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 CAEEL])</td></tr>
-<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=3k6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6t OCA], [http://pdbe.org/3k6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k6t RCSB], [http://www.ebi.ac.uk/pdbsum/3k6t PDBsum]</span></td></tr>
+<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=3k6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6t OCA], [http://pdbe.org/3k6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k6t RCSB], [http://www.ebi.ac.uk/pdbsum/3k6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6t ProSAT]</span></td></tr>
 </table>
 == Function ==

3k6t

From Proteopedia

Revision as of 08:27, 1 November 2017

Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans at 2.04 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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