2b6g: Difference between revisions

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[[Image:2b6g.gif|left|200px]]


{{Structure
==RNA recognition by the Vts1 SAM domain==
|PDB= 2b6g |SIZE=350|CAPTION= <scene name='initialview01'>2b6g</scene>
<StructureSection load='2b6g' size='340' side='right'caption='[[2b6g]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
<table><tr><td colspan='2'>[[2b6g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B6G FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE= Vts1p ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6g OCA], [https://pdbe.org/2b6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b6g RCSB], [https://www.ebi.ac.uk/pdbsum/2b6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6g ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[2d3d|2D3D]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6g OCA], [http://www.ebi.ac.uk/pdbsum/2b6g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b6g RCSB]</span>
[https://www.uniprot.org/uniprot/VTS1_YEAST VTS1_YEAST] RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs. May be involved in vacuolar protein transport.<ref>PMID:11445562</ref> <ref>PMID:12858164</ref>
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''RNA recognition by the Vts1 SAM domain'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/2b6g_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2b6g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p-SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop.
The putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p-SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop.


==About this Structure==
RNA recognition by the Vts1p SAM domain.,Johnson PE, Donaldson LW Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:16429155<ref>PMID:16429155</ref>
2B6G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6G OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
RNA recognition by the Vts1p SAM domain., Johnson PE, Donaldson LW, Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16429155 16429155]
</div>
<div class="pdbe-citations 2b6g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Donaldson LW]]
[[Category: Donaldson, L W.]]
[[Category: Johnson PE]]
[[Category: Johnson, P E.]]
[[Category: alpha-helix]]
[[Category: hairpin]]
[[Category: pentaloop]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:12 2008''

Latest revision as of 12:23, 22 May 2024

RNA recognition by the Vts1 SAM domainRNA recognition by the Vts1 SAM domain

Structural highlights

2b6g is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VTS1_YEAST RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs. May be involved in vacuolar protein transport.[1] [2]

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 putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p-SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop.

RNA recognition by the Vts1p SAM domain.,Johnson PE, Donaldson LW Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:16429155[3]

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

References

  1. ↑ Dilcher M, Kohler B, von Mollard GF. Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. J Biol Chem. 2001 Sep 14;276(37):34537-44. Epub 2001 Jul 9. PMID:11445562 doi:http://dx.doi.org/10.1074/jbc.M101551200
  2. ↑ Aviv T, Lin Z, Lau S, Rendl LM, Sicheri F, Smibert CA. The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators. Nat Struct Biol. 2003 Aug;10(8):614-21. PMID:12858164 doi:10.1038/nsb956
  3. ↑ Johnson PE, Donaldson LW. RNA recognition by the Vts1p SAM domain. Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:16429155 doi:10.1038/nsmb1039
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