6nyy | pdb_00006nyy

human m-AAA protease AFG3L2, substrate-bound

Loading... Status: waiting for Mol* initialization Structural highlights 6nyy is a 10 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, ANP, MG, ZN Gene: AFG3L2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [AFG32_HUMAN] Spinocerebellar ataxia type 28;Early-onset spastic ataxia-neuropathy syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function [AFG32_HUMAN] ATP-dependent protease which is essential for axonal development (By similarity). Publication Abstract from PubMed Mitochondrial AAA+ quality-control proteases regulate diverse aspects of mitochondrial biology through specialized protein degradation, but the underlying mechanisms of these enzymes remain poorly defined. The mitochondrial AAA+ protease AFG3L2 is of particular interest, as genetic mutations localized throughout AFG3L2 are linked to diverse neurodegenerative disorders. However, a lack of structural data has limited our understanding of how mutations impact enzymatic function. Here, we used cryoelectron microscopy (cryo-EM) to determine a substrate-bound structure of the catalytic core of human AFG3L2. This structure identifies multiple specialized structural features that integrate with conserved motifs required for ATP-dependent translocation to unfold and degrade targeted proteins. Many disease-relevant mutations localize to these unique structural features of AFG3L2 and distinctly influence its activity and stability. Our results provide a molecular basis for neurological phenotypes associated with different AFG3L2 mutations and establish a structural framework to understand how different members of the AAA+ superfamily achieve specialized biological functions. Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.,Puchades C, Ding B, Song A, Wiseman RL, Lander GC, Glynn SE Mol Cell. 2019 Jul 11. pii: S1097-2765(19)30472-1. doi:, 10.1016/j.molcel.2019.06.016. PMID:31327635 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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