PDBsum entry 1hqo

Signaling protein

PDB id: 1hqo

Contents

Protein chains

227 a.a. *

Waters ×204

* Residue conservation analysis

PDB id:

1hqo

Name:

Signaling protein

Title:

Crystal structure of the nitrogen regulation fragment of the yeast prion protein ure2p

Structure:

Ure2 protein. Chain: a, b. Fragment: nitrogen regulation fragment. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: ure2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.30Å R-factor: 0.221 R-free: 0.275

Authors:

T.C.Umland,K.L.Taylor,S.Rhee,R.B.Wickner,D.R.Davies

Key ref:

T.C.Umland et al. (2001). The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc Natl Acad Sci U S A, 98, 1459-1464. PubMed id: 11171973 DOI: 10.1073/pnas.041607898

Date:

18-Dec-00 Release date: 14-Feb-01

Protein chains

P23202  (URE2_YEAST) -  Transcriptional regulator URE2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 354 a.a.

Struc: 227 a.a.

Enzyme reactions

• Enzyme class 1: E.C.1.11.1.9 - glutathione peroxidase.
• Reaction: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
• Cofactor: Se(2+)
• Enzyme class 2: E.C.1.8.4.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1073/pnas.041607898

Proc Natl Acad Sci U S A 98:1459-1464 (2001)

PubMed id: 11171973

The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.

T.C.Umland, K.L.Taylor, S.Rhee, R.B.Wickner, D.R.Davies.

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.

Selected figure(s)

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.

Figures were selected by an automated process.