 |
PDBsum entry 1hqo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
1hqo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The crystal structure of the nitrogen regulation fragment of the yeast prion protein ure2p.
|
|
|
Authors
|
|
T.C.Umland,
K.L.Taylor,
S.Rhee,
R.B.Wickner,
D.R.Davies.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 2001,
98,
1459-1464.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
is due to a prion form of the nitrogen
regulatory protein Ure2p. It is a negative regulator of nitrogen catabolism and
acts by inhibiting the transcription factor Gln3p. Ure2p residues 1--80 are
necessary for prion generation and propagation. The C-terminal fragment retains
nitrogen regulatory activity, albeit somewhat less efficiently than the
full-length protein, and it also lowers the frequency of prion generation. The
crystal structure of this C-terminal fragment, Ure2p(97--354), at 2.3 A
resolution is described here. It adopts the same fold as the glutathione
S-transferase superfamily, consistent with their sequence similarity. However,
Ure2p(97--354) lacks a properly positioned catalytic residue that is required
for S-transferase activity. Residues within this regulatory fragment that have
been indicated by mutational studies to influence prion generation have been
mapped onto the three-dimensional structure, and possible implications for prion
activity are discussed.
|
|
|
|
|
|
|
|
Figure 1.
Fig. 1. Stereoview of the Ure2p(97-354). Monomer A is
green and Monomer B is cyan. Prion-inhibiting regions (His-151
to Ser-158 and Val-347 to Glu-354) are indicated in blue, and
the prion-promoting region (Ser-221 to Ile-227) is indicated in
red. Gold labels the position of two additional residues
implicated in affecting prion-induction, K127 and V271.
|
|
Figure 4.
Fig. 4. The superposition of Monomer A of Ure2p(97-354)
(red) and a monomer of A. thaliana GST (38) (blue). This
representation is viewed into the cleft between the two domains,
which in GST contains the G- and H-sites.
|
|
|
|
|
|
|
|
|
|
