2woj

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<StructureSection load='2woj' size='340' side='right'caption='[[2woj]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='2woj' size='340' side='right'caption='[[2woj]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2woj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WOJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2woj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WOJ FirstGlance]. <br>
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</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>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.994&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arsenite-transporting_ATPase Arsenite-transporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.16 3.6.3.16] </span></td></tr>
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<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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2woj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2woj OCA], [https://pdbe.org/2woj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2woj RCSB], [https://www.ebi.ac.uk/pdbsum/2woj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2woj ProSAT]</span></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=2woj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2woj OCA], [https://pdbe.org/2woj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2woj RCSB], [https://www.ebi.ac.uk/pdbsum/2woj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2woj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GET3_YEAST GET3_YEAST]] 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 GET1 and GET2, 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 GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.<ref>PMID:12680698</ref> <ref>PMID:16269340</ref> <ref>PMID:18724936</ref> <ref>PMID:21866104</ref> <ref>PMID:21719644</ref>
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[https://www.uniprot.org/uniprot/GET3_YEAST GET3_YEAST] 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 GET1 and GET2, 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 GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.<ref>PMID:12680698</ref> <ref>PMID:16269340</ref> <ref>PMID:18724936</ref> <ref>PMID:21866104</ref> <ref>PMID:21719644</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2woj ConSurf].
</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=2woj ConSurf].
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Targeting of newly synthesized membrane proteins to the endoplasmic reticulum is an essential cellular process. Most membrane proteins are recognized and targeted co-translationally by the signal recognition particle. However, nearly 5% of membrane proteins are 'tail-anchored' by a single carboxy-terminal transmembrane domain that cannot access the co-translational pathway. Instead, tail-anchored proteins are targeted post-translationally by a conserved ATPase termed Get3. The mechanistic basis for tail-anchored protein recognition or targeting by Get3 is not known. Here we present crystal structures of yeast Get3 in 'open' (nucleotide-free) and 'closed' (ADP.AlF(4)(-)-bound) dimer states. In the closed state, the dimer interface of Get3 contains an enormous hydrophobic groove implicated by mutational analyses in tail-anchored protein binding. In the open state, Get3 undergoes a striking rearrangement that disrupts the groove and shields its hydrophobic surfaces. These data provide a molecular mechanism for nucleotide-regulated binding and release of tail-anchored proteins during their membrane targeting by Get3.
 
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The structural basis of tail-anchored membrane protein recognition by Get3.,Mateja A, Szlachcic A, Downing ME, Dobosz M, Mariappan M, Hegde RS, Keenan RJ Nature. 2009 Sep 17;461(7262):361-6. Epub 2009 Aug 12. PMID:19675567<ref>PMID:19675567</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2woj" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arsenite-transporting ATPase]]
 
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dobosz, M]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Downing, M E]]
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[[Category: Dobosz M]]
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[[Category: Hegde, R S]]
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[[Category: Downing ME]]
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[[Category: Keenan, R J]]
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[[Category: Hegde RS]]
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[[Category: Mariappan, M]]
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[[Category: Keenan RJ]]
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[[Category: Mateja, A]]
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[[Category: Mariappan M]]
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[[Category: Szlachcic, A]]
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[[Category: Mateja A]]
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[[Category: Arsa]]
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[[Category: Szlachcic A]]
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[[Category: Arsenical resistance]]
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[[Category: Arsenite]]
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[[Category: Atp-binding]]
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[[Category: Atpase]]
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[[Category: Cytoplasm]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Er-golgi transport]]
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[[Category: Get3]]
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[[Category: Golgi apparatus]]
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[[Category: Hydrolase]]
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[[Category: Membrane protein]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Tail-anchored]]
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[[Category: Targeting factor]]
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[[Category: Transport]]
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[[Category: Trc40]]
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Current revision

ADP-AlF4 complex of S. cerevisiae GET3

PDB ID 2woj

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