3A7P
The crystal structure of Saccharomyces cerevisiae Atg16
Summary for 3A7P
| Entry DOI | 10.2210/pdb3a7p/pdb |
| Related | 3A7O |
| Descriptor | Autophagy protein 16 (2 entities in total) |
| Functional Keywords | coiled-coil, autophagy, coiled coil, cytoplasmic vesicle, protein transport, transport, vacuole |
| Biological source | Saccharomyces cerevisiae (yeast) |
| Cellular location | Preautophagosomal structure membrane ; Peripheral membrane protein : Q03818 |
| Total number of polymer chains | 2 |
| Total formula weight | 34607.21 |
| Authors | Fujioka, Y.,Noda, N.N.,Inagaki, F. (deposition date: 2009-10-01, release date: 2009-11-03, Last modification date: 2023-11-01) |
| Primary citation | Fujioka, Y.,Noda, N.N.,Nakatogawa, H.,Ohsumi, Y.,Inagaki, F. Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy. J.Biol.Chem., 285:1508-1515, 2010 Cited by PubMed Abstract: Atg16 interacts with the Atg12-Atg5 protein conjugate through its N-terminal domain and self-assembles through its coiled-coil domain (CCD). Formation of the Atg12-Atg5.Atg16 complex is essential for autophagy, the bulk degradation process conserved among most eukaryotes. Here, we report the crystal structures of full-length Saccharomyces cerevisiae Atg16 at 2.8 A resolution and its CCD at 2.5 A resolution. The CCD and full-length Atg16 each exhibit an extended alpha-helix, 90 and 130 A, respectively, and form a parallel coiled-coil dimer in the crystals. Although the apparent molecular weight of Atg16 observed by gel-filtration chromatography suggests that Atg16 is tetrameric, an analytical ultracentrifugation study showed Atg16 as a dimer in solution, consistent with the crystal structure. Evolutionary conserved surface residues clustered at the C-terminal half of Atg16 CCD were shown to be crucial for autophagy. These results will give a structural basis for understanding the molecular functions and significance of Atg16 in autophagy. PubMed: 19889643DOI: 10.1074/jbc.M109.053520 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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