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Título: | Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin |
Autor: | Gómez-Llorente, Yacob; Jebara, Fady; Patra, Malay; Malik, Radhika; Nisemblat, Shahar; Chomsky-Hecht, Orna; Parnas, Avital; Azem, Abdussalam; Hirsch, Joel A.; Ubarretxena, Iban | Palabras clave: | Biochemistry Structural biology |
Fecha de publicación: | 21-abr-2020 | Editor: | Nature Publishing Group | Citación: | Nature Communications 11: 1916 (2020) | Resumen: | mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins without the negative ATP binding inter-ring cooperativity of GroEL-GroES. Here we report the crystal structure of an ATP (ADP:BeF3-bound) ground-state mimic double-ring mHsp6014-(mHsp107)2 football complex, and the cryo-EM structures of the ADP-bound successor mHsp6014-(mHsp107)2 complex, and a single-ring mHsp607-mHsp107 half-football. The structures explain the nucleotide dependence of mHsp60 ring formation, and reveal an inter-ring nucleotide symmetry consistent with the absence of negative cooperativity. In the ground-state a two-fold symmetric H-bond and a salt bridge stitch the double-rings together, whereas only the H-bond remains as the equatorial gap increases in an ADP football poised to split into half-footballs. Refolding assays demonstrate obligate single- and double-ring mHsp60 variants are active, and complementation analysis in bacteria shows the single-ring variant is as efficient as wild-type mHsp60. Our work provides a structural basis for active single- and double-ring complexes coexisting in the mHsp60-mHsp10 chaperonin reaction cycle. | Versión del editor: | https://doi.org/10.1038/s41467-020-15698-8 | URI: | http://hdl.handle.net/10261/339526 | DOI: | 10.1038/s41467-020-15698-8 | E-ISSN: | 2041-1723 |
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Structural_basis_Gomez_Llorente.pdf | 4,58 MB | Adobe PDF | Visualizar/Abrir |
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