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| | {{STRUCTURE_1g6y| PDB=1g6y | SCENE= }} | | {{STRUCTURE_1g6y| PDB=1g6y | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTIEN URE2 FROM YEAST SACCHAROMYCES CEREVISIAE'''
| + | ===CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTIEN URE2 FROM YEAST SACCHAROMYCES CEREVISIAE=== |
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| - | ==Overview==
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| - | BACKGROUND: The [URE3] non-Mendelian element of the yeast S. cerevisiae is due to the propagation of a transmissible form of the protein Ure2. The infectivity of Ure2p is thought to originate from a conformational change of the normal form of the prion protein. This conformational change generates a form of Ure2p that assembles into amyloid fibrils. Hence, knowledge of the three-dimensional structure of prion proteins such as Ure2p should help in understanding the mechanism of amyloid formation associated with a number of neurodegenerative diseases. RESULTS: Here we report the three-dimensional crystal structure of the globular region of Ure2p (residues 95--354), also called the functional region, solved at 2.5 A resolution by the MAD method. The structure of Ure2p 95--354 shows a two-domain protein forming a globular dimer. The N-terminal domain is composed of a central 4 strand beta sheet flanked by four alpha helices, two on each side. In contrast, the C-terminal domain is entirely alpha-helical. The fold of Ure2p 95--354 resembles that of the beta class glutathione S-transferases (GST), in line with a weak similarity in the amino acid sequence that exists between these proteins. Ure2p dimerizes as GST does and possesses a potential ligand binding site, although it lacks GST activity. CONCLUSIONS: The structure of the functional region of Ure2p is the first crystal structure of a prion protein. Structure comparisons between Ure2p 95--354 and GST identified a 32 amino acid residues cap region in Ure2p exposed to the solvent. The cap region is highly flexible and may interact with the N-terminal region of the partner subunit in the dimer. The implication of this interaction in the assembly of Ure2p into amyloid fibrils is discussed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11342133}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11342133 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11342133}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Gst superfamily]] | | [[Category: Gst superfamily]] |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:13:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:48:01 2008'' |
Revision as of 01:48, 1 July 2008
Template:STRUCTURE 1g6y
CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTIEN URE2 FROM YEAST SACCHAROMYCES CEREVISIAE
Template:ABSTRACT PUBMED 11342133
About this Structure
1G6Y is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae., Bousset L, Belrhali H, Janin J, Melki R, Morera S, Structure. 2001 Jan 10;9(1):39-46. PMID:11342133
Page seeded by OCA on Tue Jul 1 04:48:01 2008
