PMID:7925981

Citation	Iwamoto, A, Orita-Saita, Y, Maeda, M and Futai, M (1994) N-ethylmaleimide-sensitive mutant (beta Val-153-->Cys) Escherichia coli F1-ATPase: cross-linking of the mutant beta subunit with the alpha subunit. FEBS Lett. 352:243-6
Abstract	A beta subunit mutation, beta Val-153-->Cys, in the glycine-rich sequence (phosphate-binding loop) of Escherichia coli F1 was constructed. Like vacuolar-type ATPase, the mutant enzyme was inhibited by N-ethylmaleimide (NEM) and labeled with [14C]NEM. The inhibition and labeling were prevented by ATP. m-Maleimidobenzoyl-N-hydroxysuccinimide (MBS) (3 microM) almost completely inhibited the mutant enzyme, and cross-linked one pair of alpha and beta subunits. These results suggest that the interaction of the domain near beta Val-153 with the alpha subunit is essential for catalytic cooperativity of the enzyme and that beta Val-153 is within 10 A of the alpha subunit.
Links	PubMed
Keywords	Adenosine Triphosphate/pharmacology; Amino Acid Sequence; Cross-Linking Reagents/pharmacology; Cysteine/metabolism; Escherichia coli/enzymology; Ethylmaleimide/pharmacology; Molecular Sequence Data; Mutation/physiology; Proton-Translocating ATPases/antagonists & inhibitors; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/genetics; Succinimides/pharmacology
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