Helicase structure and mechanism

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 clar...

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Veröffentlicht in:Current Opinion in Structural Biology 2002-02, Vol.12 (1), p.123-133
Hauptverfasser: Caruthers, Jonathan M, McKay, David B
Format: Artikel
Sprache:eng
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Zusammenfassung: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. The expanding database of helicase structures, enzymes that catalyse the separation of duplex oligonucleotides into single strands, has clarified the structural themes and variations that relate the different families.
ISSN:0959-440X
1879-033X
DOI:10.1016/S0959-440X(02)00298-1