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1stu

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Revision as of 07:53, 14 March 2018

DOUBLE STRANDED RNA BINDING DOMAIN

Structural highlights

1stu is a 1 chain structure with sequence from Drome. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DOUBLE STRANDED RNA BINDING DO (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[STAU_DROME] Required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. Osk protein is required to keep osk RNA and stau protein at the posterior pole. Stau-bcd complexes form particles that show a microtubule-dependent localization.^[1] ^[2] ^[3]

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

The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid motif that is found in a variety of proteins that interact with double-stranded (ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase, PKR. Drosophila staufen protein contains five copies of this motif, and the third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR methods, we have determined that staufen dsRBD3 forms a compact protein domain with an alpha-beta-beta-beta-alpha structure in which the two alpha-helices lie on one face of a three-stranded anti-parallel beta-sheet. This structure is very similar to that of the N-terminal domain of a prokaryotic ribosomal protein S5. Furthermore, the consensus derived from all known S5p family sequences shares several conserved residues with the dsRBD consensus sequence, indicating that the two domains share a common evolutionary origin. Using in vitro mutagenesis, we have identified several surface residues which are important for the RNA binding of the dsRBD, and these all lie on the same side of the domain. Two residues that are essential for RNA binding, F32 and K50, are also conserved in the S5 protein family, suggesting that the two domains interact with RNA in a similar way.

NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.,Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D EMBO J. 1995 Jul 17;14(14):3563-71. PMID:7628456^[4]

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

References

↑ St Johnston D, Beuchle D, Nusslein-Volhard C. Staufen, a gene required to localize maternal RNAs in the Drosophila egg. Cell. 1991 Jul 12;66(1):51-63. PMID:1712672
↑ Ferrandon D, Elphick L, Nusslein-Volhard C, St Johnston D. Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner. Cell. 1994 Dec 30;79(7):1221-32. PMID:8001156
↑ Ramos A, Grunert S, Adams J, Micklem DR, Proctor MR, Freund S, Bycroft M, St Johnston D, Varani G. RNA recognition by a Staufen double-stranded RNA-binding domain. EMBO J. 2000 Mar 1;19(5):997-1009. PMID:10698941 doi:10.1093/emboj/19.5.997
↑ Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 1995 Jul 17;14(14):3563-71. PMID:7628456

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/1stu"

Categories: Drome | Bycroft, M | Double stranded rna binding domain | Staufen

@@ Line 1: / Line 1: @@
 ==DOUBLE STRANDED RNA BINDING DOMAIN==
 <StructureSection load='1stu' size='340' side='right' caption='[[1stu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1stu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1STU FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DOUBLE STRANDED RNA BINDING DO ([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=1stu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1stu OCA], [http://pdbe.org/1stu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1stu RCSB], [http://www.ebi.ac.uk/pdbsum/1stu 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=1stu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1stu OCA], [http://pdbe.org/1stu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1stu RCSB], [http://www.ebi.ac.uk/pdbsum/1stu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1stu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1stu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1stu_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1stu

From Proteopedia

Revision as of 07:53, 14 March 2018

DOUBLE STRANDED RNA BINDING DOMAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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