The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion.
Tail-anchored (TA) proteins represent a unique class of membrane proteins that contain a single C-terminal transmembrane helix. The post-translational insertion of the yeast TA proteins into the ER membrane requires the Golgi ER trafficking (GET) complex which contains Get1, Get2 and Get3. Get3 is a...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2009-11-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2778870?pdf=render |
| _version_ | 1818418245866094592 |
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| author | Junbin Hu Jingzhi Li Xinguo Qian Vlad Denic Bingdong Sha |
| author_facet | Junbin Hu Jingzhi Li Xinguo Qian Vlad Denic Bingdong Sha |
| author_sort | Junbin Hu |
| collection | DOAJ |
| description | Tail-anchored (TA) proteins represent a unique class of membrane proteins that contain a single C-terminal transmembrane helix. The post-translational insertion of the yeast TA proteins into the ER membrane requires the Golgi ER trafficking (GET) complex which contains Get1, Get2 and Get3. Get3 is an ATPase that recognizes and binds the C-terminal transmembrane domain (TMD) of the TA proteins. We have determined the crystal structures of Get3 from two yeast species, S. cerevisiae and D. hansenii, respectively. These high resolution crystal structures show that Get3 contains a nucleotide-binding domain and a "finger" domain for binding the TA protein TMD. A large hydrophobic groove on the finger domain of S. cerevisiae Get3 structure might represent the binding site for TMD of TA proteins. A hydrophobic helix from a symmetry-related Get3 molecule sits in the TMD-binding groove and mimics the TA binding scenario. Interestingly, the crystal structures of the Get3 dimers from S. cerevisiae and D. hansenii exhibit distinct conformations. The S. cerevisiae Get3 dimer structure does not contain nucleotides and maintains an "open" conformation, while the D. hansenii Get3 dimer structure binds ADP and stays in a "closed" conformation. We propose that the conformational changes to switch the Get3 between the open and closed conformations may facilitate the membrane insertions for TA proteins. |
| first_indexed | 2024-12-14T12:19:37Z |
| format | Article |
| id | doaj.art-505be3fabaa2491aa4cd4420c22a8379 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-14T12:19:37Z |
| publishDate | 2009-11-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-505be3fabaa2491aa4cd4420c22a83792022-12-21T23:01:33ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-11-01411e806110.1371/journal.pone.0008061The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion.Junbin HuJingzhi LiXinguo QianVlad DenicBingdong ShaTail-anchored (TA) proteins represent a unique class of membrane proteins that contain a single C-terminal transmembrane helix. The post-translational insertion of the yeast TA proteins into the ER membrane requires the Golgi ER trafficking (GET) complex which contains Get1, Get2 and Get3. Get3 is an ATPase that recognizes and binds the C-terminal transmembrane domain (TMD) of the TA proteins. We have determined the crystal structures of Get3 from two yeast species, S. cerevisiae and D. hansenii, respectively. These high resolution crystal structures show that Get3 contains a nucleotide-binding domain and a "finger" domain for binding the TA protein TMD. A large hydrophobic groove on the finger domain of S. cerevisiae Get3 structure might represent the binding site for TMD of TA proteins. A hydrophobic helix from a symmetry-related Get3 molecule sits in the TMD-binding groove and mimics the TA binding scenario. Interestingly, the crystal structures of the Get3 dimers from S. cerevisiae and D. hansenii exhibit distinct conformations. The S. cerevisiae Get3 dimer structure does not contain nucleotides and maintains an "open" conformation, while the D. hansenii Get3 dimer structure binds ADP and stays in a "closed" conformation. We propose that the conformational changes to switch the Get3 between the open and closed conformations may facilitate the membrane insertions for TA proteins.http://europepmc.org/articles/PMC2778870?pdf=render |
| spellingShingle | Junbin Hu Jingzhi Li Xinguo Qian Vlad Denic Bingdong Sha The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. PLoS ONE |
| title | The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. |
| title_full | The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. |
| title_fullStr | The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. |
| title_full_unstemmed | The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. |
| title_short | The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. |
| title_sort | crystal structures of yeast get3 suggest a mechanism for tail anchored protein membrane insertion |
| url | http://europepmc.org/articles/PMC2778870?pdf=render |
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