Trans-interface coupling in the tetrameric enzyme underlies allosteric control in Escherichia coli biosynthetic threonine deaminase
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Allosteric regulation in biosynthetic L-threonine deaminase (BTD) has long been attributed to effector-induced conformational changes. Here, we identify a trans-interface coupling mechanism that regulates the active site architecture of EcIlvA, the BTD homolog... ...
