1NYH

Crystal Structure of the Coiled-coil Dimerization Motif of Sir4

Summary for 1NYH

• Entry DOI: 10.2210/pdb1nyh/pdb
• Descriptor: Regulatory protein SIR4 (1 entity in total)
• Functional Keywords: coiled-coil, transcription regulation, repressor, transcription repressor
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P11978
• Total number of polymer chains: 1
• Total formula weight: 18652.97

Authors

Chang, J.F.,Hall, B.E.,Tanny, J.C.,Moazed, D.,Filman, D.,Ellenberger, T. (deposition date: 2003-02-12, release date: 2003-06-24, Last modification date: 2024-02-14)

Primary citation

Chang, J.F.,Hall, B.E.,Tanny, J.C.,Moazed, D.,Filman, D.,Ellenberger, T.
Structure of the Coiled-coil Dimerization Motif of Sir4 and Its Interaction With Sir3
Structure, 11:637-649, 2003

PubMed Abstract: The yeast silent information regulators Sir2, Sir3, and Sir4 physically interact with one another to establish a transcriptionally silent state by forming repressive chromatin structures. The Sir4 protein contains binding sites for both Sir2 and Sir3, and these protein-protein interactions are required for gene silencing. Here, we report the X-ray structure of the coiled-coil dimerization motif within the C-terminus of Sir4 and show that it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues 464-978). We have identified a cluster of residues on the surface of the Sir4 coiled coil required for specific interactions with Sir3. The histone deacetylase Sir2 can also bind to this complex, forming a ternary complex with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4 with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to chromatin by virtue of its interactions with Sir4 and with deacetylated histones in chromatin.

PubMed: 12791253
DOI: 10.1016/S0969-2126(03)00093-5

Experimental method

X-RAY DIFFRACTION (3.1 Å)