1zv1

From Proteopedia

(Difference between revisions)

Revision as of 08:14, 10 September 2015

Crystal structure of the dimerization domain of doublesex protein from D. melanogaster

Structural highlights

1zv1 is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	dsx (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[DSX_DROME] Controls somatic sexual differentiation. Binds directly and specifically to the FBE (fat body enhancer) of the yolk protein 1 and 2 genes (Yp1 and Yp2). This enhancer is sufficient to direct the female-specific transcription characteristic of the Yp genes in adult fat bodies. Involved in regulation of male-specific expression of takeout in brain-associated fat body.^[1]

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

Male- and female-specific isoforms of the Doublesex (DSX) transcription factor regulate somatic sexual differentiation in Drosophila. The isoforms (DSX(M) and DSX(F)) share an N-terminal DNA binding domain (the DM motif), broadly conserved among metazoan sex-determining pathways. DM-DNA recognition is enhanced by a C-terminal dimerization domain. The crystal structure of this domain, determined at a resolution of 1.6 A, reveals a novel dimeric arrangement of ubiquitin-associated (UBA) folds. Although this alpha-helical motif is well characterized in pathways of DNA repair and subcellular trafficking, to our knowledge this is its first report in a transcription factor. Dimerization is mediated by a non-canonical hydrophobic interface extrinsic to the putative ubiquitin binding surface. Key side chains at this interface, identified by alanine scanning mutagenesis, are conserved among DSX homologs. The mechanism of dimerization is thus unrelated to the low affinity domain swapping observed among ubiquitin-associated CUE domains. The unexpected observation of a ubiquitin-associated fold in DSX extends the repertoire of alpha-helical dimerization elements in transcription factors. The possibility that the ubiquitination machinery participates in the regulation of sexual dimorphism is discussed.

Dimerization of doublesex is mediated by a cryptic ubiquitin-associated domain fold: implications for sex-specific gene regulation.,Bayrer JR, Zhang W, Weiss MA J Biol Chem. 2005 Sep 23;280(38):32989-96. Epub 2005 Jul 27. PMID:16049008^[2]

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

References

↑ Dauwalder B, Tsujimoto S, Moss J, Mattox W. The Drosophila takeout gene is regulated by the somatic sex-determination pathway and affects male courtship behavior. Genes Dev. 2002 Nov 15;16(22):2879-92. PMID:12435630 doi:http://dx.doi.org/10.1101/gad.1010302
↑ Bayrer JR, Zhang W, Weiss MA. Dimerization of doublesex is mediated by a cryptic ubiquitin-associated domain fold: implications for sex-specific gene regulation. J Biol Chem. 2005 Sep 23;280(38):32989-96. Epub 2005 Jul 27. PMID:16049008 doi:http://dx.doi.org/10.1074/jbc.M507990200

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/1zv1"

@@ Line 2: / Line 2: @@
 <StructureSection load='1zv1' size='340' side='right' caption='[[1zv1]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zv1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZV1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zv1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZV1 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=1zv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zv1 RCSB], [http://www.ebi.ac.uk/pdbsum/1zv1 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=1zv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zv1 OCA], [http://pdbe.org/1zv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zv1 RCSB], [http://www.ebi.ac.uk/pdbsum/1zv1 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1zv1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Drosophila melanogaster]]
+[[Category: Drome]]
 [[Category: Bayrer, J R]]
 [[Category: Li, B]]

1zv1

From Proteopedia

Revision as of 08:14, 10 September 2015

Crystal structure of the dimerization domain of doublesex protein from D. melanogaster

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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