3M95
Crystal structure of autophagy-related protein Atg8 from the silkworm Bombyx mori
Summary for 3M95
Entry DOI | 10.2210/pdb3m95/pdb |
Descriptor | Autophagy related protein Atg8 (2 entities in total) |
Functional Keywords | alpha slash beta, receptor, transport protein |
Biological source | Bombyx mori (Silk moth) |
Total number of polymer chains | 2 |
Total formula weight | 29890.13 |
Authors | Teng, Y.-B.,Hu, C.,Zhang, X.,Jiang, Y.L.,Hu, H.-X.,Zhou, C.Z. (deposition date: 2010-03-20, release date: 2010-07-21, Last modification date: 2023-11-01) |
Primary citation | Hu, C.,Zhang, X.,Teng, Y.-B.,Hu, H.-X.,Li, W.-F. Structure of autophagy-related protein Atg8 from the silkworm Bombyx mori Acta Crystallogr.,Sect.F, 66:787-790, 2010 Cited by PubMed Abstract: Autophagy-related protein Atg8 is ubiquitous in all eukaryotes. It is involved in the Atg8-PE ubiquitin-like conjugation system, which is essential for autophagosome formation. The structures of Atg8 from different species are very similar and share a ubiquitin-fold domain at the C-terminus. In the 2.40 A crystal structure of Atg8 from the silkworm Bombyx mori reported here, the ubiquitin fold at the C-terminus is preceded by two additional helices at the N-terminus. PubMed: 20606273DOI: 10.1107/S1744309110018464 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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