2PFV
S. cerevisiae Exo70 with additional residues to 2.1 Angrstrom resolution
Summary for 2PFV
| Entry DOI | 10.2210/pdb2pfv/pdb |
| Related | 2B1E 2B7M |
| Descriptor | Exocyst complex component EXO70 (2 entities in total) |
| Functional Keywords | helix-turn-helix, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle : P19658 |
| Total number of polymer chains | 1 |
| Total formula weight | 64621.54 |
| Authors | Moore, B.A.,Robinson, H.H.,Xu, Z. (deposition date: 2007-04-05, release date: 2007-05-22, Last modification date: 2024-02-21) |
| Primary citation | Moore, B.A.,Robinson, H.H.,Xu, Z. The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst. J.Mol.Biol., 371:410-421, 2007 Cited by PubMed Abstract: The exocyst is a eukaryotic tethering complex necessary for the fusion of exocytic vesicles with the plasma membrane. Its function in vivo is tightly regulated by interactions with multiple small GTPases. Exo70, one of the eight subunits of the exocyst, is important for the localization of the exocyst to the plasma membrane. It interacts with TC10 and Rho3 GTPases in mammals and yeast, respectively, and has been shown recently to bind to the actin-polymerization complex Arp2/3. Here, we present the crystal structure of Mus musculus Exo70 at 2.25 A resolution. Exo70 is composed of alpha-helices in a series of right-handed helix-turn-helix motifs organized into a long rod of length 170 A and width 35 A. Although the alpha-helical organization of this molecule is similar to that in Saccharomyces cerevisiae Exo70, major structural differences are observed on the surface of the molecule, at the domain boundaries, and in various loop structures. In particular, the C-terminal domain of M. musculus Exo70 adopts a new orientation relative to the N-terminal half not seen in S. cerevisiae Exo70 structures. Given the low level of sequence conservation within Exo70, this structure provides new insights into our understanding of many species-specific functions of the exocyst. PubMed: 17583731DOI: 10.1016/j.jmb.2007.05.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
