By Roland Benz
This primary publication devoted to the subject relates the identified physiological services of porins to their molecular constitution and mechanism, as documented by way of numerous in vitro and in vivo tools, together with the iteration of null mutants in mice. For the 1st time, it brings jointly biophysical facts with reviews played in a mobile context, featuring a unified photograph of the elemental significance of porins for mobile functionality. With sixteen contributions via an interdisciplinary group of top porin researchers, this reference is key interpreting for each molecular or structural biologist with an curiosity during this crucial protein relatives.
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Extra resources for Bacterial and Eukaryotic Porins: Structure, Function, Mechanism
Such a conformational change would then modulate protein function, for example, by increasing affinity for DNA. When over-expressed in vivo, OmpR T83I is unable to activate transcription of either ompF or ompC. This defect is not due to a defect in phosphorylation by EnvZ. DNase I footprinting assays indicated that the OmpRT83I mutant was able to bind to ompF DNA identically to wild-type OmpR, yet displayed altered binding at ompC. Thus, OmpR must adopt different conformations when bound to ompF versus ompC.
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