5WLP
Solution structure of the pseudo-receiver domain of Atg32
Summary for 5WLP
| Entry DOI | 10.2210/pdb5wlp/pdb |
| NMR Information | BMRB: 27081 |
| Descriptor | Autophagy-related protein 32 (1 entity in total) |
| Functional Keywords | atg32, pseudo-receiver domain, protein transport |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 16742.61 |
| Authors | Xue, X.,Pellegrini, M.,Ragusa, M.J. (deposition date: 2017-07-27, release date: 2018-07-04, Last modification date: 2024-05-15) |
| Primary citation | Xia, X.,Katzenell, S.,Reinhart, E.F.,Bauer, K.M.,Pellegrini, M.,Ragusa, M.J. A pseudo-receiver domain in Atg32 is required for mitophagy. Autophagy, 14:1620-1628, 2018 Cited by PubMed Abstract: Mitochondria are targeted for degradation by mitophagy, a selective form of autophagy. In Saccharomyces cerevisiae, mitophagy is dependent on the autophagy receptor, Atg32, an outer mitochondrial membrane protein. Once activated, Atg32 recruits the autophagy machinery to mitochondria, facilitating mitochondrial capture in phagophores, the precursors to autophagosomes. However, the mechanism of Atg32 activation remains poorly understood. To investigate this crucial step in mitophagy regulation, we examined the structure of Atg32. We have identified a structured domain in Atg32 that is essential for the initiation of mitophagy, as it is required for the proteolysis of the C-terminal domain of Atg32 and the subsequent recruitment of Atg11. The solution structure of this domain was determined by NMR spectroscopy, revealing that Atg32 contains a previously undescribed pseudo-receiver (PsR) domain. Our data suggests that the PsR domain of Atg32 regulates Atg32 activation and the initiation of mitophagy. PubMed: 29909755DOI: 10.1080/15548627.2018.1472838 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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