title: XPB: An essential helicase involved in both transcription and repair of DNA.
abstract: Helicases are molecular motors known to unwind double-stranded DNA. In a recent issue of Molecular Cell, Fan et al. (2006) revealed the core structure of XPB helicase, a component of transcription factor IIH, and proposed a mechanism for its dual role in transcription and nucleotide excision repair.
authors.affiliation: Macromolecular Crystallography Group, European Synchrotron Radiation Facility, B.P. 220, 6 rue Jules Horowitz, F-38043, Grenoble-Cedex 9, France.
authors.forename: Joanna
authors.initials: J
authors.lastname: Timmins
authors.forename: Sean
authors.initials: S
authors.lastname: McSweeney
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019611:Archaeoglobus fulgidus / Q000737:chemistry; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000378:metabolism*; D004252:DNA Mutational Analysis; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
chemical_list: D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; D020409:Molecular Motor Proteins; D004265:DNA Helicases