4CO7
Crystal structure of human GATE-16
Summary for 4CO7
| Entry DOI | 10.2210/pdb4co7/pdb |
| Descriptor | GAMMA-AMINOBUTYRIC ACID RECEPTOR-ASSOCIATED PROTEIN-LIKE 2 (2 entities in total) |
| Functional Keywords | protein transport, autophagy, beta-grasp fold, ubiquitin superfamily |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Golgi apparatus : P60520 |
| Total number of polymer chains | 2 |
| Total formula weight | 27661.93 |
| Authors | Weiergraeber, O.H.,Ma, P.,Willbold, D. (deposition date: 2014-01-27, release date: 2015-01-14, Last modification date: 2023-12-20) |
| Primary citation | Ma, P.,Schillinger, O.,Schwarten, M.,Lecher, J.,Hartmann, R.,Stoldt, M.,Mohrluder, J.,Olubiyi, O.,Strodel, B.,Willbold, D.,Weiergraber, O.H. Conformational Polymorphism in Autophagy-Related Protein Gate-16. Biochemistry, 54:5469-, 2015 Cited by PubMed Abstract: Autophagy is a fundamental homeostatic process in eukaryotic organisms, fulfilling essential roles in development and adaptation to stress. Among other factors, formation of autophagosomes critically depends on proteins of the Atg8 (autophagy-related protein 8) family, which are reversibly conjugated to membrane lipids. We have applied X-ray crystallography, nuclear magnetic resonance spectroscopy, and molecular dynamics simulations to study the conformational dynamics of Atg8-type proteins, using GATE-16 (Golgi-associated ATPase enhancer of 16 kDa), also known as GABARAPL2, as a model system. This combination of complementary approaches provides new insight into a structural transition centered on the C-terminus, which is crucial for the biological activity of these proteins. PubMed: 26284781DOI: 10.1021/ACS.BIOCHEM.5B00366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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