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3ibg
From Proteopedia
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| - | [[Image:3ibg.png|left|200px]] | ||
| - | + | ==Crystal structure of Aspergillus fumigatus Get3 with bound ADP== | |
| + | <StructureSection load='3ibg' size='340' side='right'caption='[[3ibg]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ibg]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IBG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3IBG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenite-transporting_ATPase Arsenite-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.16 3.6.3.16] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ibg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ibg OCA], [http://pdbe.org/3ibg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ibg RCSB], [http://www.ebi.ac.uk/pdbsum/3ibg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ibg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GET3_ASPFU GET3_ASPFU]] ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity).[HAMAP-Rule:MF_03112] | ||
| + | == 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/ib/3ibg_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=3ibg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Get3 ATPase directs the delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (ER). TA-proteins are characterized by having a single transmembrane helix (TM) at their extreme C terminus and include many essential proteins, such as SNAREs, apoptosis factors, and protein translocation components. These proteins cannot follow the SRP-dependent co-translational pathway that typifies most integral membrane proteins; instead, post-translationally, these proteins are recognized and bound by Get3 then delivered to the ER in the ATP dependent Get pathway. To elucidate a molecular mechanism for TA protein binding by Get3 we have determined three crystal structures in apo and ADP forms from Saccharomyces cerevisae (ScGet3-apo) and Aspergillus fumigatus (AfGet3-apo and AfGet3-ADP). Using structural information, we generated mutants to confirm important interfaces and essential residues. These results point to a model of how Get3 couples ATP hydrolysis to the binding and release of TA-proteins. | ||
| - | + | Model for eukaryotic tail-anchored protein binding based on the structure of Get3.,Suloway CJ, Chartron JW, Zaslaver M, Clemons WM Jr Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14849-54. Epub 2009 Aug 14. PMID:19706470<ref>PMID:19706470</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ibg" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[ATPase|ATPase]] | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Arsenite-transporting ATPase]] | [[Category: Arsenite-transporting ATPase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Chartron, J W | + | [[Category: Chartron, J W]] |
| - | [[Category: Clemons, W M | + | [[Category: Clemons, W M]] |
| - | [[Category: Suloway, C J.M | + | [[Category: Suloway, C J.M]] |
| - | [[Category: Zaslaver, M | + | [[Category: Zaslaver, M]] |
[[Category: Deviant walker a motif]] | [[Category: Deviant walker a motif]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Nucleotide binding]] | [[Category: Nucleotide binding]] | ||
Current revision
Crystal structure of Aspergillus fumigatus Get3 with bound ADP
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