 |
PDBsum entry 5flm
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
5flm
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
1427 a.a.
|
|
|
|
|
|
|
|
|
|
|
1134 a.a.
|
|
|
|
|
|
|
|
|
|
|
257 a.a.
|
|
|
|
|
|
|
|
|
|
|
128 a.a.
|
|
|
|
|
|
|
|
|
|
|
209 a.a.
|
|
|
|
|
|
|
|
|
|
|
82 a.a.
|
|
|
|
|
|
|
|
|
|
|
171 a.a.
|
|
|
|
|
|
|
|
|
|
|
148 a.a.
|
|
|
|
|
|
|
|
|
|
|
114 a.a.
|
|
|
|
|
|
|
|
|
|
|
67 a.a.
|
|
|
|
|
|
|
|
|
|
|
115 a.a.
|
|
|
|
|
|
|
|
|
|
|
44 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of transcribing mammalian RNA polymerase ii.
|
|
|
Authors
|
|
C.Bernecky,
F.Herzog,
W.Baumeister,
J.M.Plitzko,
P.Cramer.
|
|
|
Ref.
|
|
Nature, 2016,
529,
551-554.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
RNA polymerase (Pol) II produces messenger RNA during transcription of
protein-coding genes in all eukaryotic cells. The Pol II structure is known at
high resolution from X-ray crystallography for two yeast species. Structural
studies of mammalian Pol II, however, remain limited to low-resolution electron
microscopy analysis of human Pol II and its complexes with various proteins.
Here we report the 3.4 Å resolution cryo-electron microscopy structure of
mammalian Pol II in the form of a transcribing complex comprising DNA template
and RNA transcript. We use bovine Pol II, which is identical to the human enzyme
except for seven amino-acid residues. The obtained atomic model closely
resembles its yeast counterpart, but also reveals unknown features. Binding of
nucleic acids to the polymerase involves 'induced fit' of the mobile Pol II
clamp and active centre region. DNA downstream of the transcription bubble
contacts a conserved 'TPSA motif' in the jaw domain of the Pol II subunit RPB5,
an interaction that is apparently already established during transcription
initiation. Upstream DNA emanates from the active centre cleft at an angle of
approximately 105° with respect to downstream DNA. This position of upstream
DNA allows for binding of the general transcription elongation factor DSIF
(SPT4-SPT5) that we localize over the active centre cleft in a conserved
position on the clamp domain of Pol II. Our results define the structure of
mammalian Pol II in its functional state, indicate that previous
crystallographic analysis of yeast Pol II is relevant for understanding gene
transcription in all eukaryotes, and provide a starting point for a mechanistic
analysis of human transcription.
|
|
|
|
|
|
|
