By Eric J. Toone
This e-book covers important advances in enzymology, explaining the habit of enzymes and the way they are often applied to increase novel medicinal drugs, synthesize identified and novel compounds, and comprehend evolutionary strategies.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology (Volume 77)
2. As mentioned above, the structure of the adaptor proteins used in modeling lacked the extreme N-terminus and a large C-terminal domain, the portion known to be essential for the interaction between the adaptor and the RND pump protein. 3. The stoichiometric ratio between the adaptor and the pump protein (or TolC–OprM) within the tripartite complex was not known. A giant stride in this area was recently made by the Koronakis group (53). They have refined the data obtained previously for the MexA crystal (47) and succeeded in obtaining the structure of the hitherto missing domain containing the N-terminus and the large C-terminal segment.
Routine assays relied on the proton eflux determined with the intravesicular pH indicator pyranine, as described above. It was soon discovered that no acceleration of proton flux occurred, with aminoglycosides (70 mM) either outside or inside vesicles, unless AcrA (with the lipidation site removed) was added at the time of reconstitution, and thus to the interior of the vesicles. It was known that AcrA was required for the activity of AcrD in intact cells (77), but this was expected because AcrA (or one of its homologs) would be needed for the construction of a tripartite efflux machinery.
Changing residues that appeared to be interacting with the ligands into alanine through site-directed mutagenesis produced a drastic decrease in resistance to most drugs in the case of Glu673, and more modest, yet significant, decreases with Phe666 and Phe664. C) are not inconsistent with the hypothesis that this is the portal for the periplasmic entry of substrates. The putative pathway for the drugs to the binding site is closed in the “access protomer” (see below), which resembles the protomers in the symmetric trimer in conformation; thus, the drug molecules cannot go further and may be forced to interact with the entrance of this pathway in the symmetric structure.
Advances in Enzymology and Related Areas of Molecular Biology (Volume 77) by Eric J. Toone