2fvu
From Proteopedia
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Structure of the yeast Sir3 BAH domain
Overview
Previous work has shown that the N terminus of the Saccharomyces, cerevisiae Sir3 protein is crucial for the function of Sir3 in, transcriptional silencing. Here, we show that overexpression of N-terminal, fragments of Sir3 in strains lacking the full-length protein can lead to, some silencing of HML and HMR. Sir3 contains a BAH (bromo-adjacent, homology) domain at its N terminus. Overexpression of this domain alone, can lead to silencing as long as Sir1 is overexpressed and Sir2 and Sir4, are present. Overexpression of the closely related Orc1 BAH domain can, also silence in the absence of any Sir3 protein. A previously, characterized hypermorphic sir3 mutation, D205N, greatly improves, silencing by the Sir3 BAH domain and allows it to bind to DNA and, oligonucleosomes in vitro. A previously uncharacterized region in the Sir1, N terminus is required for silencing by both the Sir3 and Orc1 BAH, domains. The structure of the Sir3 BAH domain has been determined. In the, crystal, the molecule multimerizes in the form of a left-handed, superhelix. This superhelix may be relevant to the function of the BAH, domain of Sir3 in silencing.
About this Structure
2FVU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and function of the Saccharomyces cerevisiae Sir3 BAH domain., Connelly JJ, Yuan P, Hsu HC, Li Z, Xu RM, Sternglanz R, Mol Cell Biol. 2006 Apr;26(8):3256-65. PMID:16581798
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