Identification of α‐subunit Lys201 and β‐subunit Lys115 at the ATP‐binding sites inEscherichia coli F1‐ATPase
- 20 June 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 233 (2), 347-351
- https://doi.org/10.1016/0014-5793(88)80457-5
Abstract
Binding of about 1 mol of adenosine triphosphopyridoxal to Escherichia coli F1-ATPase resulted in the nearly complete inactivation of the enzyme [(1987) J. Biol. Chem. 262, 7686–7692]. About two thirds of the label was bound to the α-subunit, and the rest to the β-subunit. The present study revealed that Lys201 in the α-subunit and Lys155 in the glycinerich region of the β-subunit are the major sites labeled with this reagent. Thus, these two residues might be located close to the γ-phosphate of the bound ATP.Keywords
This publication has 30 references indexed in Scilit:
- Adenosine di-, tri- and tetraphosphopyridoxals modify the same lysyl residue at the ATP-binding site in adenylate kinaseFEBS Letters, 1988
- ß‐Subunit of Escherichia coli F1‐ATPaseFEBS Letters, 1987
- Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal.Biochemistry, 1986
- Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondriaJournal of Molecular Biology, 1985
- Homology of the .gamma. subunit of phosphorylase b kinase with cAMP-dependent protein kinaseBiochemistry, 1984
- Characterization of two nucleotide binding sites on the isolated, reconstitutively active .beta. subunit of the F0.cntdot.F1 ATP synthaseBiochemistry, 1984
- The proton-ATPase of bacteria and mitochondriaThe Journal of Membrane Biology, 1983
- STRUCTURE AND FUNCTION OF H+‐ATPase: WHAT WE HAVE LEARNED FROM Escherichia coli H+‐ATPase*Annals of the New York Academy of Sciences, 1982
- The interactions of coupling ATPases with nucleotidesBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- Substrate positions and induced-fit in crystalline adenylate kinaseJournal of Molecular Biology, 1977