6vzf | pdb_00006vzf

Crystal Structure of Atg11 Coiled-Coil 3

spinqualitylabelsall models 6vzf, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vzf is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Gene: ATG11, CVT9, YPR049C, YP9499.07c (ATCC 18824) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ATG11_YEAST] Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation, through its interaction with ATG32. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for ATG9 anterograde transport from the mitochondria to the PAS. Recruits also the ATG19-prAPE1 complex to the PAS. Required for the Cvt vesicles completion. Plays a significant role in life span extension. Publication Abstract from PubMed Selective autophagy is the capture of specific cytosolic contents in double membrane vesicles that subsequently fuse with the vacuole or lysosome, thereby delivering cargo for degradation. Selective autophagy receptors (SARs) mark the cargo for degradation and, in yeast, recruit Atg11, the scaffolding protein for selective autophagy initiation. The mitochondrial protein Atg32 is the yeast SAR that mediates mitophagy, the selective autophagic capture of mitochondria. Atg11-Atg32 interactions concentrate Atg32 into puncta that are thought to represent sites of mitophagy initiation. However, it is unclear how Atg11 concentrates Atg32 to generate mitophagy initiation sites. We show here that the coiled coil 3 (CC3) domain of Atg11 is required for concentrating Atg32 into puncta. We determined the structure of the majority of the CC3, demonstrating that the CC3 forms a parallel homodimer whose dimer interface is formed by a small number of hydrophobic residues. We further show that the CC3 interface is not required for Atg11 dimerization but is required for shaping Atg32 into functional mitophagy initiation sites and for delivery of mitochondria to the vacuole. Our findings suggest that Atg11 self-interactions help concentrate SARs as a necessary precondition for cargo capture. The Third Coiled Coil Domain of Atg11 Is Required for Shaping Mitophagy Initiation Sites.,Margolis HK, Katzenell S, Leary KA, Ragusa MJ J Mol Biol. 2020 Sep 4. pii: S0022-2836(20)30528-3. doi:, 10.1016/j.jmb.2020.08.025. PMID:32896530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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