1oxj: Difference between revisions

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<StructureSection load='1oxj' size='340' side='right' caption='[[1oxj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1oxj' size='340' side='right' caption='[[1oxj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oxj]] is a 1 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=1OXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OXJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oxj]] is a 1 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=1OXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OXJ FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMG ([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">SMG ([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=1oxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oxj RCSB], [http://www.ebi.ac.uk/pdbsum/1oxj 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=1oxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxj OCA], [http://pdbe.org/1oxj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oxj RCSB], [http://www.ebi.ac.uk/pdbsum/1oxj PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1oxj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drome]]
[[Category: Aggarwal, A K]]
[[Category: Aggarwal, A K]]
[[Category: Gardner, C D]]
[[Category: Gardner, C D]]

Revision as of 13:15, 11 September 2015

Crystal structure of the Smaug RNA binding domainCrystal structure of the Smaug RNA binding domain

Structural highlights

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

Function

[SMG_DROME] Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevent their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup.[1] [2] [3] [4]

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 Nanos protein gradient in Drosophila, required for proper abdominal segmentation, is generated in part via translational repression of its mRNA by Smaug. We report here the crystal structure of the Smaug RNA binding domain, which shows no sequence homology to any previously characterized RNA binding motif. The structure reveals an unusual makeup in which a SAM domain, a common protein-protein interaction module, is affixed to a pseudo-HEAT repeat analogous topology (PHAT) domain. Unexpectedly, we find through a combination of structural and genetic analysis that it is primarily the SAM domain that interacts specifically with the appropriate nanos mRNA regulatory sequence. Therefore, in addition to their previously characterized roles in protein-protein interactions, some SAM domains play crucial roles in RNA binding.

RNA recognition via the SAM domain of Smaug.,Green JB, Gardner CD, Wharton RP, Aggarwal AK Mol Cell. 2003 Jun;11(6):1537-48. PMID:12820967[5]

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

See Also

References

  1. Dahanukar A, Walker JA, Wharton RP. Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila. Mol Cell. 1999 Aug;4(2):209-18. PMID:10488336
  2. Smibert CA, Lie YS, Shillinglaw W, Henzel WJ, Macdonald PM. Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro. RNA. 1999 Dec;5(12):1535-47. PMID:10606265
  3. Smibert CA, Wilson JE, Kerr K, Macdonald PM. smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo. Genes Dev. 1996 Oct 15;10(20):2600-9. PMID:8895661
  4. Nelson MR, Leidal AM, Smibert CA. Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression. EMBO J. 2004 Jan 14;23(1):150-9. Epub 2003 Dec 11. PMID:14685270 doi:http://dx.doi.org/10.1038/sj.emboj.7600026
  5. Green JB, Gardner CD, Wharton RP, Aggarwal AK. RNA recognition via the SAM domain of Smaug. Mol Cell. 2003 Jun;11(6):1537-48. PMID:12820967

1oxj, resolution 1.80Å

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