5WLP

Solution structure of the pseudo-receiver domain of Atg32

5WLP の概要

• エントリーDOI: 10.2210/pdb5wlp/pdb
• NMR情報: BMRB: 27081
• 分子名称: Autophagy-related protein 32 (1 entity in total)
• 機能のキーワード: atg32, pseudo-receiver domain, protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16742.61

構造登録者

Xue, X.,Pellegrini, M.,Ragusa, M.J. (登録日: 2017-07-27, 公開日: 2018-07-04, 最終更新日: 2024-05-15)

主引用文献

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

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: 29909755
DOI: 10.1080/15548627.2018.1472838

実験手法

SOLUTION NMR