PMID:7713884
| Citation |
Chang, YY and Cronan, JE Jr (1995) Detection by site-specific disulfide cross-linking of a conformational change in binding of Escherichia coli pyruvate oxidase to lipid bilayers. J. Biol. Chem. 270:7896-901 |
|---|---|
| Abstract |
Escherichia coli pyruvate oxidase, a peripheral membrane homotetrameric flavoprotein, exposes its C-terminal lipid binding site in the presence of substrate pyruvate and co-factor thiamine pyrophosphate Mg2+ and binds tightly to phospholipid bilayers during catalysis. Using site-specific disulfide cross-linking, we demonstrate that disulfide cross-links are formed between C termini of D560C pyruvate oxidase and that the degree of cross-linking is greatly increased by the presence of substrate and co-factors indicating a conformational change that results in juxtaposition of two subunit C termini. The cross-linked oxidase is enzymatically active and remains able to associate with lipid micelles. These results argue strongly that lipid bilayer binding of pyruvate oxidase involves pairing of the C termini of two subunits. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Cross-Linking Reagents/chemistry; Cysteine/chemistry; DNA Primers; Disulfides/chemistry; Escherichia coli/enzymology; Lactobacillus/enzymology; Lipid Bilayers; Lipid Metabolism; Molecular Sequence Data; Protein Conformation; Pyruvate Oxidase/chemistry; Pyruvate Oxidase/metabolism; Sequence Homology, Amino Acid |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.