Repeated tertiary fold of RNA polymerase II and implications for DNA binding.
X-ray diffraction data from two forms of yeast RNA polymerase II crystals indicate that the two largest subunits of the polymerase, Rpb1 and Rpb2, may have similar folds, as is suggested by secondary structure predictions. DNA may bind between the two subunits with its 2-fold axis aligned to a pseudo 2-fold axis of the protein.
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
J
J
Fu
M
M
Gerstein
P R
PR
David
A L
AL
Gnatt
D A
DA
Bushnell
A M
AM
Edwards
R D
RD
Kornberg
D000595:Amino Acid Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012319:RNA Polymerase II / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction; D015003:Yeasts / Q000201:enzymology
D005656:Fungal Proteins; D004247:DNA; D012319:RNA Polymerase II