Abstract
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.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Bacterial Proteins / genetics*
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Escherichia coli Proteins*
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Membrane Proteins*
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Membranes / metabolism
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Protein Conformation
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Proton-Translocating ATPases / biosynthesis*
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Proton-Translocating ATPases / genetics*
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Protons
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Membrane Proteins
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Protons
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Adenosine Triphosphate
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Proton-Translocating ATPases
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AtpH protein, E coli