1zbx
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(New page: 200px<br /><applet load="1zbx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zbx, resolution 2.5Å" /> '''Crystal structure of ...)
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Revision as of 05:15, 21 November 2007
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Crystal structure of a Orc1p-Sir1p complex
Overview
The interaction between silence information regulator 1 protein (Sir1p), and origin recognition complex 1 protein (Orc1p), the largest subunit of, the origin recognition complex, plays an important role in the, establishment of transcriptional silencing at the cryptic mating-type gene, loci in Saccharomyces cerevisiae. Sir1p binds the N-terminal region of, Orc1p encompassing a Bromo-adjacent homology (BAH) domain found in various, chromatin-associated proteins. To understand the molecular mechanism of, Sir protein recruitment, we have determined a 2.5-A cocrystal structure of, the N-terminal domain of Orc1p in complex with the Orc1p-interacting, domain of Sir1p. The structure reveals that Sir1p Orc1p-interacting domain, has a bilobal structure: an alpha/beta N-terminal lobe and a C-terminal, lobe resembling the Tudor domain royal family fold. The N-terminal lobe of, Sir1p binds in a shallow groove between a helical subdomain and the BAH, domain of Orc1p. The structure provides a mechanistic understanding of, Orc1p-Sir1p interaction specificity, as well as insights into, protein-protein interactions involving BAH domains in general.
About this Structure
1ZBX is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for origin recognition complex 1 protein-silence information regulator 1 protein interaction in epigenetic silencing., Hsu HC, Stillman B, Xu RM, Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8519-24. Epub 2005 Jun 3. PMID:15937111
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