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 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.
Soultanas
P
P
Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
Wigley
D B
DB
D001426:Bacterial Proteins; D004265:DNA Helicases / Q000737:chemistry / Q000502:physiology*; D004277:DNA, Single-Stranded / Q000378:metabolism; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013381:Subtilisins / Q000737:chemistry / Q000502:physiology; D015534:Trans-Activators; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology
D001426:Bacterial Proteins; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; C102527:PrcA protein, bacteria; D011506:Proteins; D015534:Trans-Activators; D014764:Viral Proteins; C045264:replication initiator protein; D013381:Subtilisins; D004265:DNA Helicases