1zbx
From Proteopedia
(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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- | [[Image:1zbx.gif|left|200px]]<br /><applet load="1zbx" size=" | + | [[Image:1zbx.gif|left|200px]]<br /><applet load="1zbx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zbx, resolution 2.5Å" /> | caption="1zbx, resolution 2.5Å" /> | ||
'''Crystal structure of a Orc1p-Sir1p complex'''<br /> | '''Crystal structure of a Orc1p-Sir1p complex'''<br /> | ||
==Overview== | ==Overview== | ||
- | The interaction between silence information regulator 1 protein (Sir1p) | + | 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== | ==About this Structure== | ||
- | 1ZBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1ZBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZBX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
- | [[Category: Hsu, H | + | [[Category: Hsu, H C.]] |
[[Category: Stillman, B.]] | [[Category: Stillman, B.]] | ||
- | [[Category: Xu, R | + | [[Category: Xu, R M.]] |
[[Category: epigenetics]] | [[Category: epigenetics]] | ||
[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
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[[Category: silent information regulators]] | [[Category: silent information regulators]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:04 2008'' |
Revision as of 14:14, 21 February 2008
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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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