6VKL
Negative stain reconstruction of the yeast exocyst octameric complex.
Summary for 6VKL
| Entry DOI | 10.2210/pdb6vkl/pdb |
| EMDB information | 21226 6827 |
| Descriptor | Exocyst complex component SEC3, Exocyst complex component SEC5, Exocyst complex component SEC6, ... (8 entities in total) |
| Functional Keywords | exocyst, coiled-coil, exocytosis |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 8 |
| Total formula weight | 845691.45 |
| Authors | Frost, A.,Munson, M. (deposition date: 2020-01-21, release date: 2020-07-29, Last modification date: 2024-03-06) |
| Primary citation | Rossi, G.,Lepore, D.,Kenner, L.,Czuchra, A.B.,Plooster, M.,Frost, A.,Munson, M.,Brennwald, P. Exocyst structural changes associated with activation of tethering downstream of Rho/Cdc42 GTPases. J. Cell Biol., 219:-, 2020 Cited by PubMed Abstract: The exocyst complex plays a critical role in determining both temporal and spatial dynamics of exocytic vesicle tethering and fusion with the plasma membrane. However, the mechanism by which the exocyst functions and how it is regulated remain poorly understood. Here we describe a novel biochemical assay for the examination of exocyst function in vesicle tethering. Importantly, the assay is stimulated by gain-of-function mutations in the Exo70 component of the exocyst, selected for their ability to bypass Rho/Cdc42 activation in vivo. Single-particle electron microscopy and 3D reconstructions of negatively stained exocyst complexes reveal a structural change in the mutant exocyst that exposes a binding site for the v-SNARE. We demonstrate a v-SNARE requirement in our tethering assay and increased v-SNARE binding to exocyst gain-of-function complexes. Together, these data suggest an allosteric mechanism for activation involving a conformational change in one subunit of the complex, which is relayed through the complex to regulate its biochemical activity in vitro, as well as overall function in vivo. PubMed: 31904797DOI: 10.1083/jcb.201904161 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (15 Å) |
Structure validation
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