5WHG
Vms1 mitochondrial localization core
Summary for 5WHG
| Entry DOI | 10.2210/pdb5whg/pdb |
| Descriptor | Protein VMS1, ZINC ION (3 entities in total) |
| Functional Keywords | ros signalling, oxidative stress, mitochondrial quality control, dna binding protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 44909.11 |
| Authors | Fredrickson, E.K.,Schubert, H.L.,Rutter, J.,Hill, C.P. (deposition date: 2017-07-17, release date: 2017-11-15, Last modification date: 2024-11-20) |
| Primary citation | Nielson, J.R.,Fredrickson, E.K.,Waller, T.C.,Rendon, O.Z.,Schubert, H.L.,Lin, Z.,Hill, C.P.,Rutter, J. Sterol Oxidation Mediates Stress-Responsive Vms1 Translocation to Mitochondria. Mol. Cell, 68:673-685.e6, 2017 Cited by PubMed Abstract: Vms1 translocates to damaged mitochondria in response to stress, whereupon its binding partner, Cdc48, contributes to mitochondrial protein homeostasis. Mitochondrial targeting of Vms1 is mediated by its conserved mitochondrial targeting domain (MTD), which, in unstressed conditions, is inhibited by intramolecular binding to the Vms1 leucine-rich sequence (LRS). Here, we report a 2.7 Å crystal structure of Vms1 that reveals that the LRS lies in a hydrophobic groove in the autoinhibited MTD. We also demonstrate that the oxidized sterol, ergosterol peroxide, is necessary and sufficient for Vms1 localization to mitochondria, through binding the MTD in an interaction that is competitive with binding to the LRS. These data support a model in which stressed mitochondria generate an oxidized sterol receptor that recruits Vms1 to support mitochondrial protein homeostasis. PubMed: 29149595DOI: 10.1016/j.molcel.2017.10.022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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