3vlc: Difference between revisions

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-{{STRUCTURE_3vlc|  PDB=3vlc  |  SCENE=  }}
+==Crystal structure of S. cerevisiae Get3 in the semi open conformation in complex with Get1 cytosolic domain at 4.5 angstrom resolution==
-===Crystal structure of S. cerevisiae Get3 in the semi open conformation in complex with Get1 cytosolic domain at 4.5 angstrom resolution===
+<StructureSection load='3vlc' size='340' side='right' caption='[[3vlc]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
-{{ABSTRACT_PUBMED_22684149}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3vlc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VLC FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GET1, MDM39, YGL020C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=3vlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vlc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vlc RCSB], [http://www.ebi.ac.uk/pdbsum/3vlc PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Tail-anchored (TA) proteins are integral membrane proteins that possess a single transmembrane domain near their carboxy terminus. TA proteins play critical roles in many important cellular processes such as membrane trafficking, protein translocation, and apoptosis. The GET complex mediates posttranslational insertion of newly synthesized TA proteins to the endoplasmic reticulum membrane. The GET complex is composed of the homodimeric Get3 ATPase and its heterooligomeric receptor, Get1/2. During insertion, the Get3 dimer shuttles between open and closed conformational states, coupled with ATP hydrolysis and the binding/release of TA proteins. We report crystal structures of ADP-bound Get3 in complex with the cytoplasmic domain of Get1 (Get1CD) in open and semi-open conformations at 3.0- and 4.5-A resolutions, respectively. Our structures and biochemical data suggest that Get1 uses two interfaces to stabilize the open dimer conformation of Get3. We propose that one interface is sufficient for binding of Get1 by Get3, while the second interface stabilizes the open dimer conformation of Get3.
-==Function==
+Get1 Stabilizes an Open Dimer Conformation of Get3 ATPase by Binding Two Distinct Interfaces.,Kubota K, Yamagata A, Sato Y, Goto-Ito S, Fukai S J Mol Biol. 2012 Jun 7. PMID:22684149<ref>PMID:22684149</ref>
-[[http://www.uniprot.org/uniprot/GET1_YEAST GET1_YEAST]] Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex 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 mitochondrial distribution and morphology.<ref>PMID:11907266</ref> <ref>PMID:16269340</ref> <ref>PMID:18724936</ref> <ref>PMID:21835666</ref> <ref>PMID:21719644</ref>
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[3vlc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLC OCA].
+</div>
-==Reference==
+==See Also==
-<ref group="xtra">PMID:022684149</ref><references group="xtra"/><references/>
+*[[ATPase|ATPase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Saccharomyces cerevisiae s288c]]
-[[Category: Fukai, S.]]
+[[Category: Fukai, S]]
-[[Category: Kubota, K.]]
+[[Category: Kubota, K]]
-[[Category: Yamagata, A.]]
+[[Category: Yamagata, A]]
 [[Category: Atp binding]]
 [[Category: Atpase]]