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The ATP hydrolysis\u2010defective mutant of the catalytic glutamate residue of the Walker B motif (E556Q\/E1201Q) has been used to determine the structure of the ATP\u2010bound inward\u2010closed conformation of P\u2010gp. Here, we show that this mutant does not appear to undergo the same steps as wild\u2010type P\u2010gp. We discuss conformational differences in the EQ mutant that may lead to a better understanding of the catalytic cycle of P\u2010gp and propose that additional structural studies with wild\u2010type P\u2010gp are required.<\/jats:p>","DOI":"10.1002\/1873-3468.14054","type":"journal-article","created":{"date-parts":[[2021,2,6]],"date-time":"2021-02-06T11:24:42Z","timestamp":1612610682000},"page":"750-762","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Does the ATP\u2010bound EQ mutant reflect the pre\u2010 or post\u2010ATP hydrolysis state in the catalytic cycle of human P\u2010glycoprotein (ABCB1)?"],"prefix":"10.1002","volume":"595","author":[{"given":"Sabrina","family":"Lusvarghi","sequence":"first","affiliation":[{"name":"Laboratory of Cell Biology Center for Cancer Research National Cancer Institute National Institutes of Health Bethesda MD 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