2WOO
Nucleotide-free form of S. pombe Get3
Summary for 2WOO
| Entry DOI | 10.2210/pdb2woo/pdb |
| Descriptor | ATPASE GET3, ZINC ION (2 entities in total) |
| Functional Keywords | tail-anchored, membrane protein, targeting factor, endoplasmic reticulum, get3, atpase, trc40, atp-binding, golgi apparatus, er-golgi transport, nucleotide-binding, arsenical resistance, nucleus, hydrolase, cytoplasm, transport, arsa, arsenite |
| Biological source | SCHIZOSACCHAROMYCES POMBE (FISSION YEAST) |
| Cellular location | Cytoplasm: Q9P7F8 |
| Total number of polymer chains | 6 |
| Total formula weight | 219681.50 |
| Authors | Mateja, A.,Szlachcic, A.,Downing, M.E.,Dobosz, M.,Mariappan, M.,Hegde, R.S.,Keenan, R.J. (deposition date: 2009-07-27, release date: 2009-08-11, Last modification date: 2023-12-20) |
| Primary citation | Mateja, A.,Szlachcic, A.,Downing, M.E.,Dobosz, M.,Mariappan, M.,Hegde, R.S.,Keenan, R.J. The Structural Basis of Tail-Anchored Membrane Protein Recognition by Get3. Nature, 461:361-, 2009 Cited by PubMed Abstract: 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. PubMed: 19675567DOI: 10.1038/NATURE08319 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.006 Å) |
Structure validation
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