منابع مشابه
Properties of F1-ATPase from the uncD412 mutant of Escherichia coli.
Properties of purified F1-ATPase from Escherichia coli mutant strain AN484 (uncD412) have been studied in an attempt to understand why the amino acid substitution in the beta-subunit of this enzyme causes a tenfold reduction from normal MgATP hydrolysis rate. In most properties that were studied, uncD412 F1-ATPase resembled normal E. coli F1-ATPase. Both enzymes were found to contain a total of...
متن کاملHigh-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase.
The rotary motor F(1)-ATPase from the thermophilic Bacillus PS3 (TF(1)) is one of the best-studied of all molecular machines. F(1)-ATPase is the part of the enzyme F(1)F(O)-ATP synthase that is responsible for generating most of the ATP in living cells. Single-molecule experiments have provided a detailed understanding of how ATP hydrolysis and synthesis are coupled to internal rotation within ...
متن کاملComplementation of Escherichia coli unc mutant strains by chloroplast and cyanobacterial F1-ATPase subunits.
The genes encoding the five subunits of the F1 portion of the ATPases from both spinach chloroplasts and the cyanobacterium Synechocystis sp. PCC 6803 were cloned into expression vectors and expressed in Escherichia coli. The recombinant subunits formed inclusion bodies within the cells. Each particular subunit was expressed in the respective unc mutant, each unable to grow on non-fermentable c...
متن کاملRotation of Escherichia coli F(1)-ATPase.
By applying the same method used for F(1)-ATPase (TF(1)) from thermophilic Bacillus PS3 (Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K., Jr. (1997) Nature 386, 299-302), we observed ATP-driven rotation of a fluorescent actin filament attached to the gamma subunit in Escherichia coli F(1)-ATPase. The torque value and the direction of the rotation were the same as those observed for TF(1). F...
متن کاملRole of Asn-243 in the Phosphate-binding Subdomain of Catalytic Sites of Escherichia coli F1-ATPase*
In the catalytic mechanism of ATP synthase, phosphate (Pi) binding and release steps are believed to be correlated to -subunit rotation, and Pi binding is proposed to be prerequisite for binding ADP in the face of high cellular [ATP]/[ADP] ratios. In x-ray structures, residue Asn-243 appears centrally located in the Pibinding subdomain of catalytic sites. Here we studied the role of Asn-243 in ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2013
ISSN: 0021-9258
DOI: 10.1074/jbc.m113.451583