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-Structure paper
タイトル | Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 1916, Year 2020 |
掲載日 | 2020年4月21日 |
著者 | Yacob Gomez-Llorente / Fady Jebara / Malay Patra / Radhika Malik / Shahar Nisemblat / Orna Chomsky-Hecht / Avital Parnas / Abdussalam Azem / Joel A Hirsch / Iban Ubarretxena-Belandia / |
PubMed 要旨 | 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:BeF- ...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:BeF-bound) ground-state mimic double-ring mHsp60-(mHsp10) football complex, and the cryo-EM structures of the ADP-bound successor mHsp60-(mHsp10) complex, and a single-ring mHsp60-mHsp10 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. |
リンク | Nat Commun / PubMed:32317635 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.08 - 3.82 Å |
構造データ | |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-HOH: |
由来 |
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キーワード | CHAPERONE / Complex / ADP / Football / Half-football |