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2vtg
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2vtg.jpg|left|200px]] | ||
| - | < | + | ==Crystal Structure of Human Iba2, trigonal crystal form== |
| - | + | <StructureSection load='2vtg' size='340' side='right'caption='[[2vtg]], [[Resolution|resolution]] 2.45Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2vtg]] is a 1 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=2VTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VTG 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]] 2.45Å</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=ZN:ZINC+ION'>ZN</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=2vtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vtg OCA], [https://pdbe.org/2vtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vtg RCSB], [https://www.ebi.ac.uk/pdbsum/2vtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vtg ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AIF1L_HUMAN AIF1L_HUMAN] Actin-binding protein that promotes actin bundling. May neither bind calcium nor depend on calcium for function.<ref>PMID:18699778</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/vt/2vtg_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=2vtg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Iba2 is a homolog of ionized calcium-binding adapter molecule 1 (Iba1), a 17-kDa protein that binds and cross-links filamentous actin (F-actin) and localizes to membrane ruffles and phagocytic cups. Here, we present the crystal structure of human Iba2 and its homodimerization properties, F-actin cross-linking activity, cellular localization and recruitment upon bacterial invasion in comparison with Iba1. The Iba2 structure comprises two central EF-hand motifs lacking bound Ca2+. Iba2 crystallized as a homodimer stabilized by a disulfide bridge and zinc ions. Analytical ultracentrifugation revealed a different mode of dimerization under reducing conditions that was independent of Ca2+. Furthermore, no binding of Ca2+ up to 0.1 mM was detected by equilibrium dialysis. Correspondingly, Iba EF-hand motifs lack residues essential for strong Ca2+ coordination. Sedimentation experiments and microscopy detected pronounced, indistinguishable F-actin binding and cross-linking activity of Iba1 and Iba2 with induction of F-actin bundles. Fluorescent Iba fusion proteins were expressed in HeLa cells and co-localized with F-actin. Iba1 was recruited into cellular projections to a larger extent than Iba2. Additionally, we studied Iba recruitment in a Shigella invasion model that induces cytoskeletal rearrangements. Both proteins were recruited into the bacterial invasion zone and Iba1 was again concentrated slightly higher in the cellular extensions. | ||
| - | + | Structural and functional characterization of human Iba proteins.,Schulze JO, Quedenau C, Roske Y, Adam T, Schuler H, Behlke J, Turnbull AP, Sievert V, Scheich C, Mueller U, Heinemann U, Bussow K FEBS J. 2008 Sep;275(18):4627-40. Epub 2008 Aug 11. PMID:18699778<ref>PMID:18699778</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2vtg" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
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| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Buessow | + | [[Category: Large Structures]] |
| - | [[Category: Heinemann | + | [[Category: Buessow K]] |
| - | [[Category: Mueller | + | [[Category: Heinemann U]] |
| - | [[Category: Quedenau | + | [[Category: Mueller U]] |
| - | [[Category: Roske | + | [[Category: Quedenau C]] |
| - | [[Category: Schulze | + | [[Category: Roske Y]] |
| - | [[Category: Turnbull | + | [[Category: Schulze JO]] |
| - | + | [[Category: Turnbull A]] | |
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Current revision
Crystal Structure of Human Iba2, trigonal crystal form
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Categories: Homo sapiens | Large Structures | Buessow K | Heinemann U | Mueller U | Quedenau C | Roske Y | Schulze JO | Turnbull A

