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New page: left|200px<br /><applet load="2fnj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fnj, resolution 1.800Å" /> '''Crystal structure o...
 
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[[Image:2fnj.gif|left|200px]]<br /><applet load="2fnj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2fnj, resolution 1.800&Aring;" />
'''Crystal structure of a B30.2/SPRY domain-containing protein GUSTAVUS in complex with Elongin B and Elongin C'''<br />


==Overview==
==Crystal structure of a B30.2/SPRY domain-containing protein GUSTAVUS in complex with Elongin B and Elongin C==
The B30.2/SPRY domain is present in approximately 700 eukaryotic, (approximately 150 human) proteins, including medically important proteins, such as TRIM5alpha and Pyrin. Nonetheless, the functional role of this, modular domain remained unclear. Here, we report the crystal structure of, an SPRY-SOCS box family protein GUSTAVUS in complex with Elongins B and C, revealing a highly distorted two-layered beta-sandwich core structure of, its B30.2/SPRY domain. Ensuing studies identified one end of the, beta-sandwich as the surface interacting with an RNA helicase VASA with a, 40 nM dissociation constant. The sequence variation in TRIM5alpha, responsible for HIV-1 restriction and most of the mutations in Pyrin, causing familial Mediterranean fever map on this surface, implicating the, corresponding region in many B30.2/SPRY domains as the ligand-binding, site. The amino acids lining the binding surface are highly variable among, the B30.2/SPRY domains, suggesting that these domains are, protein-interacting modules, which recognize a specific individual partner, protein rather than a consensus sequence motif.
<StructureSection load='2fnj' size='340' side='right'caption='[[2fnj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fnj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FNJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fnj OCA], [https://pdbe.org/2fnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fnj RCSB], [https://www.ebi.ac.uk/pdbsum/2fnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fnj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUS_DROME GUS_DROME] Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.<ref>PMID:12479811</ref> <ref>PMID:20123973</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fn/2fnj_consurf.spt"</scriptWhenChecked>
    <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=2fnj ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2FNJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FNJ OCA].
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
== References ==
==Reference==
<references/>
Structural and functional insights into the B30.2/SPRY domain., Woo JS, Imm JH, Min CK, Kim KJ, Cha SS, Oh BH, EMBO J. 2006 Mar 22;25(6):1353-63. Epub 2006 Feb 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16498413 16498413]
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Oh BH]]
[[Category: Oh, B.H.]]
[[Category: Woo JS]]
[[Category: Woo, J.S.]]
[[Category: b30.2]]
[[Category: beta-sandwich]]
[[Category: lectin-like]]
[[Category: spry]]
 
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