ATP-driven rotation of the gamma subunit in F(1)-ATPase.
FEBS Lett
; 483(1): 1-5, 2000 Oct 13.
Article
em En
| MEDLINE
| ID: mdl-11033345
ABSTRACT
We present a mechanism for F(1)-ATPase in which hydrolysis of MgATP in the high-affinity catalytic site at the alpha/beta interface drives rotation of the gamma subunit via conformational changes in the alpha subunit. During hydrolysis, transition state formation and separation of P(i) from MgADP causes movement of portions of alpha, transmitted via two Arg residues which are hydrogen-bonded to the gamma-phosphate of MgATP, alphaArg376 and betaArg182; the latter is also hydrogen-bonded to interfacial alpha residues between alpha346 and alpha349. Changes in alpha conformation then push on gamma, resulting in rotation. Supporting evidence from the literature and from new data is discussed.
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Base de dados:
MEDLINE
Assunto principal:
Trifosfato de Adenosina
/
ATPases Translocadoras de Prótons
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article