8hac
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==A novel dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo== | |
| - | + | <StructureSection load='8hac' size='340' side='right'caption='[[8hac]], [[Resolution|resolution]] 2.32Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8hac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaeodactylum_tricornutum_CCAP_1055/1 Phaeodactylum tricornutum CCAP 1055/1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HAC 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]] 2.32Å</td></tr> | |
| - | [[Category: | + | <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>, <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=8hac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hac OCA], [https://pdbe.org/8hac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hac RCSB], [https://www.ebi.ac.uk/pdbsum/8hac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hac ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B7G933_PHATC B7G933_PHATC] 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.[HAMAP-Rule:MF_03112] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phaeodactylum tricornutum CCAP 1055/1]] | ||
| + | [[Category: Chang HY]] | ||
| + | [[Category: Ko TP]] | ||
Current revision
A novel dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo
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