2B1E
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
Summary for 2B1E
| Entry DOI | 10.2210/pdb2b1e/pdb |
| Related | 2D2S |
| Descriptor | Exocyst complex component EXO70 (2 entities in total) |
| Functional Keywords | tethering complex, exocyst, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Bud: P19658 |
| Total number of polymer chains | 1 |
| Total formula weight | 64803.81 |
| Authors | Dong, G.,Hutagalung, A.H.,Fu, C.,Novick, P.,Reinisch, K.M. (deposition date: 2005-09-15, release date: 2005-11-01, Last modification date: 2024-03-13) |
| Primary citation | Dong, G.,Hutagalung, A.H.,Fu, C.,Novick, P.,Reinisch, K.M. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif Nat.Struct.Mol.Biol., 12:1094-1100, 2005 Cited by PubMed Abstract: The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods. PubMed: 16249794DOI: 10.1038/nsmb1017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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