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By determining the structures of RPH from\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    (LmRPH) in different conformations, we reveal a toggle-switch mechanism of the LmRPH catalytic process in which the C-terminal His domain swings between the ATP-binding domain and the rifampin-binding domain to transfer phosphate from ATP to rifampin. These structures explain the low substrate selectivity of RPH for the rifamycins. The residues involved in rifampin phosphorylation are identified also. The structural mechanism revealed in this study will guide the development of a new generation of rifamycins.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1523614113","type":"journal-article","created":{"date-parts":[[2016,3,21]],"date-time":"2016-03-21T23:56:21Z","timestamp":1458604581000},"page":"3803-3808","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":30,"title":["Structural basis of rifampin inactivation by rifampin phosphotransferase"],"prefix":"10.1073","volume":"113","author":[{"given":"Xiaofeng","family":"Qi","sequence":"first","affiliation":[{"name":"National Key Laboratory of Plant Molecular Genetics, Chinese Academy of Sciences Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China;"},{"name":"University of Chinese Academy of Sciences, Beijing 100039, 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