View source for 3zjc


==Crystal structure of GMPPNP-bound human GIMAP7 L100Q variant==
<StructureSection load='3zjc' size='340' side='right'caption='[[3zjc]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zjc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJC 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]] 3.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3zjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjc OCA], [https://pdbe.org/3zjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zjc RCSB], [https://www.ebi.ac.uk/pdbsum/3zjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zjc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GIMA7_HUMAN GIMA7_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GTPases of immunity-associated proteins (GIMAPs) are regulators of lymphocyte survival and homeostasis. We previously determined the structural basis of GTP-dependent GIMAP2 scaffold formation on lipid droplets. To understand how its GTP hydrolysis is activated, we screened for other GIMAPs on lipid droplets and identified GIMAP7. In contrast to GIMAP2, GIMAP7 displayed dimerization-stimulated GTP hydrolysis. The crystal structure of GTP-bound GIMAP7 showed a homodimer that assembled via the G domains, with the helical extensions protruding in opposite directions. We identified a catalytic arginine that is supplied to the opposing monomer to stimulate GTP hydrolysis. GIMAP7 also stimulated GTP hydrolysis by GIMAP2 via an analogous mechanism. Finally, we found GIMAP2 and GIMAP7 expression differentially regulated in several human T cell lymphoma lines. Our findings suggest that GTPase activity in the GIMAP family is controlled by homo- and heterodimerization. This may have implications for the differential roles of some GIMAPs in lymphocyte survival.

Structural Insights into the Mechanism of GTPase Activation in the GIMAP Family.,Schwefel D, Arasu BS, Marino SF, Lamprecht B, Kochert K, Rosenbaum E, Eichhorst J, Wiesner B, Behlke J, Rocks O, Mathas S, Daumke O Structure. 2013 Feb 27. pii: S0969-2126(13)00022-1. doi:, 10.1016/j.str.2013.01.014. PMID:23454188<ref>PMID:23454188</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zjc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Daumke O]]
[[Category: Schwefel D]]