1G6Y

CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTEIN URE2 FROM YEAST SACCHAROMYCES CEREVISIAE

Summary for 1G6Y

• Entry DOI: 10.2210/pdb1g6y/pdb
• Related: 1G6W
• Descriptor: URE2 PROTEIN (2 entities in total)
• Functional Keywords: gst superfamily, structural genomics
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : P23202
• Total number of polymer chains: 2
• Total formula weight: 59932.21

Authors

Bousset, L.,Belrhali, H.,Janin, J.,Melki, R.,Morera, S. (deposition date: 2000-11-08, release date: 2001-02-21, Last modification date: 2024-02-07)

Primary citation

Bousset, L.,Belrhali, H.,Janin, J.,Melki, R.,Morera, S.
Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae.
Structure, 9:39-46, 2001

PubMed Abstract: 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.

PubMed: 11342133
DOI: 10.1016/S0969-2126(00)00553-0

Experimental method

X-RAY DIFFRACTION (2.8 Å)