2E7S
Crystal structure of the yeast Sec2p GEF domain
Summary for 2E7S
| Entry DOI | 10.2210/pdb2e7s/pdb |
| Descriptor | Rab guanine nucleotide exchange factor SEC2 (2 entities in total) |
| Functional Keywords | coiled coil, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Bud neck: P17065 |
| Total number of polymer chains | 20 |
| Total formula weight | 315610.28 |
| Authors | Fukai, S.,Sato, Y.,Nureki, O. (deposition date: 2007-01-12, release date: 2007-02-27, Last modification date: 2024-10-30) |
| Primary citation | Sato, Y.,Shirakawa, R.,Horiuchi, H.,Dohmae, N.,Fukai, S.,Nureki, O. Asymmetric Coiled-Coil Structure with Guanine Nucleotide Exchange Activity Structure, 15:245-252, 2007 Cited by PubMed Abstract: Vesicular traffic during exocytosis is regulated by Rab GTPase, Sec4p in yeast, which is activated by a guanine nucleotide exchange factor (GEF) called Sec2p. The GEF activity is localized in the N-terminal 160 residues of Sec2p, which lacks sequence similarity with any other GEFs with known structures, and thereby the guanine nucleotide exchange mechanism by Sec2p remains unknown. Here, we report the crystal structure of the Sec2p GEF domain at 3.0 A resolution. The structure unexpectedly consists of a homodimeric, parallel coiled coil that extends over 180 A. Pull-down and guanine nucleotide exchange analyses on a series of deletion and point mutants of Sec2p unveiled the catalytic residues for its GEF activity as well as the Sec4p binding site, thus presenting a nucleotide exchange mechanism by a simple coiled coil. The present functional analyses allow us to build the Sec2p:Sec4p complex model, which explains the specificity for Rab GTPases by their respective GEF proteins. PubMed: 17292842DOI: 10.1016/j.str.2007.01.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
