Mutations in the delta subunit influence the assembly of F1F0 ATP synthase in Escherichia coli.
Missense mutations affecting Asp-161 and Ser-163 in the delta subunit of F1F0 ATP synthase have been generated. Although most substitutions allowed substantial enzyme function, the delta Asp-161-->Pro substitution resulted in a loss of enzyme activity. The loss of activity was attributable to a structural failure altering assembly of the enzyme complex.
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Department of Biochemistry and Molecular Biology, University of Florida, Gainesville 32610.
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D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D008566:Membranes / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000096:biosynthesis* / Q000235:genetics*; D011522:Protons; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D011522:Protons; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; C101709:AtpH protein, E coli