Structure and Function of Subunit <Emphasis Type="Italic">a</Emphasis> of the ATP Synthase of <Emphasis Type="Italic">Escherichia coli</Emphasis> |
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Authors: | Email author" target="_blank">Steven?B?VikEmail author Robert?R?Ishmukhametov |
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Institution: | (1) Department of Biological Sciences, Southern Methodist University, Dallas, Texas, 75275–0376 |
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Abstract: | The structure of subunit a of the Escherichia coli ATP synthase has been probed by construction of more than one hundred monocysteine substitutions. Surface labeling with 3-N-maleimidyl-propionyl biocytin (MPB) has defined five transmembrane helices, the orientation of the protein in the membrane,
and information about the relative exposure of the loops connecting these helices. Cross-linking studies using TFPAM-3 (N-(4-azido-2,3,5,6-tetrafluorobenzyl)-3-maleimido-propionamide) and benzophenone-4-maleimide have revealed which elements of
subunit a are near subunits b and c. Use of a chemical protease reagent, 5-(-bromoacetamido)-1,10-phenanthroline-copper, has indicated that the periplasmic end
of transmembrane helix 5 is near that of transmembrane helix 2. |
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Keywords: | ATP synthase subunit a proton translocation cysteine mutagenesis membrane topology |
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