2xtp: Difference between revisions
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[[ | ==CRYSTAL STRUCTURE OF NUCLEOTIDE-FREE HUMAN GIMAP2, AMINO ACID RESIDUES 1-260== | ||
<StructureSection load='2xtp' size='340' side='right' caption='[[2xtp]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xtp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XTP FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xtn|2xtn]], [[2xto|2xto]], [[2xtm|2xtm]]</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=2xtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xtp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xtp RCSB], [http://www.ebi.ac.uk/pdbsum/2xtp PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
GTPases of immunity-associated proteins (GIMAPs) are a distinctive family of GTPases, which control apoptosis in lymphocytes and play a central role in lymphocyte maturation and lymphocyte-associated diseases. To explore their function and mechanism, we determined crystal structures of a representative member, GIMAP2, in different nucleotide-loading and oligomerization states. Nucleotide-free and GDP-bound GIMAP2 were monomeric and revealed a guanine nucleotide-binding domain of the TRAFAC (translation factor associated) class with a unique amphipathic helix alpha7 packing against switch II. In the absence of alpha7 and the presence of GTP, GIMAP2 oligomerized via two distinct interfaces in the crystal. GTP-induced stabilization of switch I mediates dimerization across the nucleotide-binding site, which also involves the GIMAP specificity motif and the nucleotide base. Structural rearrangements in switch II appear to induce the release of alpha7 allowing oligomerization to proceed via a second interface. The unique architecture of the linear oligomer was confirmed by mutagenesis. Furthermore, we showed a function for the GIMAP2 oligomer at the surface of lipid droplets. Although earlier studies indicated that GIMAPs are related to the septins, the current structure also revealed a strikingly similar nucleotide coordination and dimerization mode as in the dynamin GTPase. Based on this, we reexamined the relationships of the septin- and dynamin-like GTPases and demonstrate that these are likely to have emerged from a common membrane-associated dimerizing ancestor. This ancestral property appears to be critical for the role of GIMAPs as nucleotide-regulated scaffolds on intracellular membranes. | |||
Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).,Schwefel D, Frohlich C, Eichhorst J, Wiesner B, Behlke J, Aravind L, Daumke O Proc Natl Acad Sci U S A. 2010 Nov 8. PMID:21059949<ref>PMID:21059949</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Daumke, O | [[Category: Daumke, O]] | ||
[[Category: Froehlich, C | [[Category: Froehlich, C]] | ||
[[Category: Schwefel, D | [[Category: Schwefel, D]] | ||
[[Category: G protein]] | [[Category: G protein]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
