4xwo
From Proteopedia
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==Structure of Get3 bound to the transmembrane domain of Sec22== | ==Structure of Get3 bound to the transmembrane domain of Sec22== | ||
| - | <StructureSection load='4xwo' size='340' side='right' caption='[[4xwo]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='4xwo' size='340' side='right'caption='[[4xwo]], [[Resolution|resolution]] 2.75Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xwo]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XWO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xwo]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XWO FirstGlance]. <br> | ||
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwo OCA], [http://pdbe.org/4xwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xwo RCSB], [http://www.ebi.ac.uk/pdbsum/4xwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xwo ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwo OCA], [http://pdbe.org/4xwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xwo RCSB], [http://www.ebi.ac.uk/pdbsum/4xwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xwo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://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> | [[http://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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==See Also== | ==See Also== | ||
| - | *[[3D structures | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| + | *[[Antibody 3D structures|Antibody 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Baker's yeast]] | [[Category: Baker's yeast]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Chang, H Y]] | [[Category: Chang, H Y]] | ||
[[Category: Hegde, R S]] | [[Category: Hegde, R S]] | ||
Revision as of 10:41, 25 December 2019
Structure of Get3 bound to the transmembrane domain of Sec22
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