DNA helicases: ‘inching forward’

Recently determined crystal structures of PcrA helicase complexed with a DNA substrate have revealed details of the helicase mechanism. PcrA and UvrD helicases have been shown to be functional as monomers, challenging previous suggestions that all helicases are required to be oligomeric. Crystal str...

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Veröffentlicht in:	Current Opinion in Structural Biology 2000-02, Vol.10 (1), p.124-128
Hauptverfasser:	Soultanas, Panos, Wigley, Dale B
Format:	Artikel
Sprache:	eng
Schlagworte:	ATPase activity Bacterial Proteins DNA helicase DNA Helicases - chemistry DNA Helicases - physiology DNA translocation DNA, Single-Stranded - metabolism DNA-Binding Proteins gene 4 Helix unwinding Hwlicase Macromolecular Substances Models, Molecular Nucleic Acid Conformation PcrA protein Protein Conformation Proteins - chemistry Proteins - physiology RepA protein Sequence Homology, Amino Acid Subtilisins - chemistry Subtilisins - physiology Trans-Activators UvrD protein Viral Proteins - chemistry Viral Proteins - physiology X-ray crystallography
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Beschreibung
Zusammenfassung:	Recently determined crystal structures of PcrA helicase complexed with a DNA substrate have revealed details of the helicase mechanism. PcrA and UvrD helicases have been shown to be functional as monomers, challenging previous suggestions that all helicases are required to be oligomeric. Crystal structures of the hexameric helicases RepA and T7 gene 4 explain the formation of hexameric assemblies from identical monomers with RecA-like folds, but their molecular mechanism remains elusive.
ISSN:	0959-440X 1879-033X
DOI:	10.1016/S0959-440X(99)00059-7