title: Helicase structure and mechanism.
abstract: Structural information on helicase proteins has expanded recently beyond the DNA helicases Rep and PcrA, and the hepatitis C virus RNA helicase to include UvrB, members of the DEA(D/H)-box RNA helicase family, examples of DnaB-related helicases and RuvB. The expanding database of structures has clarified the structural 'theme and variations' that relate the different helicase families. Furthermore, information is emerging on the functions of the conserved helicase motifs and their participation in the mechanisms by which these proteins catalyze the remodeling of DNA and RNA in ATP-dependent activities.
authors.affiliation: Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, USA.
authors.forename: Jonathan M
authors.initials: JM
authors.lastname: Caruthers
authors.forename: David B
authors.initials: DB
authors.lastname: McKay
mesh_terms: D020816:Amino Acid Motifs; D001426:Bacterial Proteins / Q000502:physiology; D017124:Conserved Sequence; D004265:DNA Helicases / Q000737:chemistry* / Q000502:physiology; D053488:DnaB Helicases; D005810:Multigene Family; D011487:Protein Conformation; D020365:RNA Helicases / Q000737:chemistry* / Q000502:physiology; D017385:Sequence Homology; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; C084217:pcrA protein, Bacteria; D004265:DNA Helicases; D053488:DnaB Helicases; D020365:RNA Helicases