The C-terminal domain revealed in the structure of RNA polymerase II.
The location of the CTD in the structure of RNA polymerase II has been determined by electron crystallography at 16 A resolution. Difference maps between wild-type enzyme and that lacking the CTD, or with an antibody fragment bound in place of the CTD, disclose the site of attachment of the CTD to the polymerase. Appropriate display of the polymerase structure reveals the CTD as an element projecting from this site of attachment into solution. A low relative density and large volume of this element identify the CTD as a conformationally mobile region.
Meredith
G D
GD
Department of Structural Biology, Stanford University School of Medicine, CA 94305-5400, USA.
Chang
W H
WH
Li
Y
Y
Bushnell
D A
DA
Darst
S A
SA
Kornberg
R D
RD
D000595:Amino Acid Sequence; D003460:Crystallization; D005583:Fourier Analysis; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012319:RNA Polymerase II / Q000737:chemistry*
D012319:RNA Polymerase II