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==Structure of the N-terminal I-BAR domain (1-259) of D.Discoideum IBARa==
<StructureSection load='4nqi' size='340' side='right'caption='[[4nqi]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nqi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NQI 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]] 2.21&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4nqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nqi OCA], [https://pdbe.org/4nqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nqi RCSB], [https://www.ebi.ac.uk/pdbsum/4nqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nqi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C7FZZ0_DICDI C7FZZ0_DICDI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Here, we analyzed the single I-BAR family member IBARa from D. discoideum. The X-ray structure of the N-terminal I-BAR domain solved at 2.2 A resolution revealed an all-alpha helical structure that self-associates into a 165 A zeppelin-shaped antiparallel dimer. The structural data are consistent with its shape in solution obtained by small-angle X-ray-scattering. Cosedimentation, fluorescence-anisotropy as well as fluorescence and electron microscopy revealed the I-BAR domain to bind preferentially to phosphoinositide-containing vesicles and drive the formation of negatively curved tubules. Immunofluorescence labelling further showed accumulation of endogenous IBARa at the tips of filopodia, the rim of constricting phagocytic cups, in foci connecting dividing cells during the final stage of cytokinesis, and most prominently at the osmoregulatory contractile vacuole (CV). Consistently, IBARa-null mutants displayed defects in CV formation and discharge, growth, phagocytosis and mitotic cell division, whereas filopodia formation was not compromised. Of note, IBARa-null mutants were also strongly impaired in cell spreading. Together, these data suggest IBARa to constitute an important regulator of numerous cellular processes intimately linked with the dynamic rearrangement of cellular membranes.

The inverse BAR-domain protein IBARa drives membrane remodelling to control osmoregulation, phagocytosis and cytokinesis.,Linkner J, Witte G, Zhao H, Junemann A, Nordholz B, Runge-Wollmann P, Lappalainen P, Faix J J Cell Sci. 2014 Jan 24. PMID:24463811<ref>PMID:24463811</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nqi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Faix J]]
[[Category: Runge-Wollmann P]]
[[Category: Witte G]]