Article ; Online: Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.
Protein science : a publication of the Protein Society
2023 Volume 32, Issue 7, Page(s) e4689
Abstract: The flexibility of the ATP synthase's β subunit promotes its role in the ATP synthase rotational mechanism, but its domains stability remains unknown. A reversible thermal unfolding of the isolated β subunit (Tβ) of the ATP synthase from Bacillus ... ...
Abstract | The flexibility of the ATP synthase's β subunit promotes its role in the ATP synthase rotational mechanism, but its domains stability remains unknown. A reversible thermal unfolding of the isolated β subunit (Tβ) of the ATP synthase from Bacillus thermophilus PS3, tracked through circular dichroism and molecular dynamics, indicated that Tβ shape transits from an ellipsoid to a molten globule through an ordered unfolding of its domains, preserving the β-sheet residual structure at high temperature. We determined that part of the stability origin of Tβ is due to a transversal hydrophobic array that crosses the β-barrel formed at the N-terminal domain and the Rossman fold of the nucleotide-binding domain (NBD), while the helix bundle of the C-terminal domain is the less stable due to the lack of hydrophobic residues, and thus the more flexible to trigger the rotational mechanism of the ATP synthase. |
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MeSH term(s) | Protein Structure, Secondary ; Hot Temperature ; Molecular Dynamics Simulation ; Adenosine Triphosphate/chemistry ; Circular Dichroism ; Protein Folding ; Protein Denaturation |
Chemical Substances | Adenosine Triphosphate (8L70Q75FXE) |
Language | English |
Publishing date | 2023-04-12 |
Publishing country | United States |
Document type | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 1106283-6 |
ISSN | 1469-896X ; 0961-8368 |
ISSN (online) | 1469-896X |
ISSN | 0961-8368 |
DOI | 10.1002/pro.4689 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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