Modification of the mitochondrial F1-ATPase ε subunit, enhancement of the ATPase activity of the IF1–F1 complex and IF1-binding dependence of the conformation of the ε subunit
نویسندگان
چکیده
Modification of the mitochondrial F1-ATPase ε subunit, enhancement of the ATPase activity of the IF1–F1 complex and IF1-binding dependence of the conformation of the ε subunit Giancarlo SOLAINI*, Alessandra BARACCA†, Edi GABELLIERI‡ and Giorgio LENAZ† *Scuola Superiore di Studi Universitari e di Perfezionamento S. Anna, Via G. Carducci, 40, 56127 Pisa, Italy, †Dipartimento di Biochimica, Universita' di Bologna, 40126 Bologna, Italy, and ‡Istituto di Biofisica del CNR, 56127 Pisa, Italy
منابع مشابه
Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F1-ATPase.
The hydrolysis of ATP by the ATP synthase in mitochondria is inhibited by a protein called IF1. Bovine IF1 has 84 amino acids, and its N-terminal inhibitory region is intrinsically disordered. In a known structure of bovine F1-ATPase inhibited with residues 1-60 of IF1, the inhibitory region from residues 1-50 is mainly α-helical and buried deeply at the α(DP)β(DP)-catalytic interface, where it...
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