Abstract：
:ATP synthases are rotary enzymes found in bacteria, chloroplasts, and mitochondria. These complexes produce the majority of cellular ATP in aerobic cells using energy from the transmembrane proton motive force established by the electron transport chain. In mitochondria, dimeric ATP synthase is essential for formation of the inner membrane cristae. While rotary catalysis in the soluble F1 region has been studied extensively by X-ray crystallography, the structure of the membrane embedded FO region remained elusive until recently. In the past few years, electron cryomicroscopy structures of mitochondrial, chloroplast, and bacterial ATP synthases have revealed the architecture of the FO region, helping to explain the mechanisms of proton translocation, dimerization of the enzyme in mitochondria, and cristae formation. These structures also show that ATP synthases exist in different conformational states, illustrating the flexibility and dynamics of the complex.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Guo H,Rubinstein JLdoi
10.1016/j.sbi.2018.08.005subject
Has Abstractpub_date
2018-10-01 00:00:00pages
71-79eissn
0959-440Xissn
1879-033Xpii
S0959-440X(18)30096-4journal_volume
52pub_type
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