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PDBsum entry 1k0b
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Gene regulation
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PDB id
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1k0b
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Contents |
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223 a.a.
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241 a.a.
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255 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of the yeast prion ure2p functional region in complex with glutathione and related compounds.
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Authors
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L.Bousset,
H.Belrhali,
R.Melki,
S.Morera.
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Ref.
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Biochemistry, 2001,
40,
13564-13573.
[DOI no: ]
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PubMed id
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Abstract
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The [URE3] phenotype in yeast Saccharomyces cerevisiae is due to an altered
prion form of Ure2p, a protein involved in nitrogen catabolism. To understand
possible conformational changes at the origin of prion propagation, we
previously solved the crystal structure of the Ure2p functional region [Bousset
et al. (2001) Structure 9, 39-46]. We showed the protein to have a fold similar
to that of the beta class of glutathione S-transferases (GSTs). Here we report
crystal structures of the Ure2p functional region (extending from residues
95-354) in complex with glutathione (GSH), the substrate of all GSTs, and two
widely used GST inhibitors, namely, S-hexylglutathione and
S-p-nitrobenzylglutathione. In a manner similar to what is observed in many
GSTs, ligand binding is not accompanied by a significant change in the
conformation of the protein. We identify one GSH and one hydrophobic
electrophile binding site per monomer as observed in all other GSTs. The sulfur
group of GSH, that conjugates electrophiles, is located near the amide group of
Asn124, allowing a hydrogen bond to be formed. Biochemical data indicate that
GSH binds to Ure2p with high affinity. Its binding affects Ure2p oligomerization
but has no effect on the assembly of the protein into amyloid fibrils. Despite
results indicating that Ure2p lacks GST activity, we propose that Ure2p is a
member of the GST superfamily that may describe a novel GST class. Our data
bring new insights into the function of the Ure2p active region.
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Secondary reference #1
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Title
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Structure of the globular region of the prion protein ure2 from the yeast saccharomyces cerevisiae.
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Authors
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L.Bousset,
H.Belrhali,
J.Janin,
R.Melki,
S.Morera.
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Ref.
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Structure, 2001,
9,
39-46.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. Stereo View of the Ure2p 95-354 DimerThe two
monomers are differently colored. The central b sheet is in red.
The 2-fold axis is in the plane of the drawing in (a), and
orthogonal to it in (b)
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The above figure is
reproduced from the cited reference
with permission from Cell Press
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