title: Hammerhead redux: does the new structure fit the old biochemical data?
abstract: The cleavage rates of 78 hammerhead ribozymes containing structurally conservative chemical modifications were collected from the literature and compared to the recently determined crystal structure of the Schistosoma mansoni hammerhead. With only a few exceptions, the biochemical data were consistent with the structure, indicating that the new structure closely resembles the transition state of the reaction. Since all the biochemical data were collected on minimal hammerheads that have a very different structure, the minimal hammerhead must be dynamic and occasionally adopt the quite different extended structure in order to cleave.
authors.affiliation: Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
authors.forename: Jennifer A
authors.initials: JA
authors.lastname: Nelson
authors.forename: Olke C
authors.initials: OC
authors.lastname: Uhlenbeck
mesh_terms: D000818:Animals; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D007700:Kinetics; D008345:Manganese / Q000737:chemistry; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018510:RNA, Helminth / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012550:Schistosoma mansoni / Q000201:enzymology / Q000235:genetics
chemical_list: D016337:RNA, Catalytic; D018510:RNA, Helminth; C427204:hammerhead ribozyme; D008345:Manganese