1nyh
From Proteopedia
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Crystal Structure of the Coiled-coil Dimerization Motif of Sir4
Overview
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.
About this Structure
1NYH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the coiled-coil dimerization motif of Sir4 and its interaction with Sir3., Chang JF, Hall BE, Tanny JC, Moazed D, Filman D, Ellenberger T, Structure. 2003 Jun;11(6):637-49. PMID:12791253
Page seeded by OCA on Tue Nov 20 22:39:39 2007
