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Here, we use poliovirus 2C and a derivative thereof to elucidate the first biochemical mechanism for this enzyme and confirm the applicability of this mechanism to other members of the enterovirus genus. Our biochemical data are consistent with a dimer forming in solution, binding to RNA, which stimulates ATPase activity by increasing the rate of hydrolysis without impacting affinity for ATP substantially. Both RNA and DNA bind to the same or overlapping site on 2C, driven by the phosphodiester backbone, but only RNA stimulates ATP hydrolysis. We propose that RNA binds to 2C driven by the backbone, with reorientation of the ribose hydroxyls occurring in a second step to form the catalytically competent state. 2C also uses a two-step mechanism for binding to ATP. Initial binding is driven by the \u03b1 and \u03b2 phosphates of ATP. In the second step, the adenine base and other substituents of ATP are used to organize the active site for catalysis. These studies provide the first biochemical description of determinants driving specificity and catalytic efficiency of a picornaviral 2C ATPase.<\/jats:p>","DOI":"10.1093\/nar\/gkac1054","type":"journal-article","created":{"date-parts":[[2022,10,26]],"date-time":"2022-10-26T16:51:15Z","timestamp":1666803075000},"page":"11775-11798","source":"Crossref","is-referenced-by-count":23,"title":["Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP"],"prefix":"10.1093","volume":"50","author":[{"given":"Calvin","family":"Yeager","sequence":"first","affiliation":[{"name":"Department of Microbiology & Immunology, University of North Carolina at Chapel Hill , Chapel Hill, NC 27599, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Griffin","family":"Carter","sequence":"additional","affiliation":[{"name":"Department of Microbiology & Immunology, University of North Carolina at Chapel Hill , Chapel Hill, NC 27599, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David W","family":"Gohara","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, St. Louis University , St. Louis, MO 63104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neela H","family":"Yennawar","sequence":"additional","affiliation":[{"name":"The Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park , PA 16802, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4055-633X","authenticated-orcid":false,"given":"Eric\u00a0J","family":"Enemark","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences , Little Rock, AR 72205, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jamie\u00a0J","family":"Arnold","sequence":"additional","affiliation":[{"name":"Department of Microbiology & Immunology, University of North Carolina at Chapel Hill , Chapel Hill, NC 27599, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7564-5642","authenticated-orcid":false,"given":"Craig E","family":"Cameron","sequence":"additional","affiliation":[{"name":"Department of Microbiology & Immunology, University of North Carolina at Chapel Hill , Chapel Hill, NC 27599, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2022,11,18]]},"reference":[{"key":"2022120608342770700_B1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1099\/0022-1317-78-1-1","article-title":"Classification of enteroviruses based on molecular and biological properties","volume":"78","author":"Hyypi\u00e4","year":"1997","journal-title":"J. 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