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 2.5&Aring;" /> '''Crystal structure of ...)
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[[Image:1zbx.gif|left|200px]]<br /><applet load="1zbx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zbx.gif|left|200px]]<br /><applet load="1zbx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zbx, resolution 2.5&Aring;" />
caption="1zbx, resolution 2.5&Aring;" />
'''Crystal structure of a Orc1p-Sir1p complex'''<br />
'''Crystal structure of a Orc1p-Sir1p complex'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZBX OCA].
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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]]
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[[Category: Hsu, H.C.]]
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[[Category: Hsu, H C.]]
[[Category: Stillman, B.]]
[[Category: Stillman, B.]]
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[[Category: Xu, R.M.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:22:25 2007''
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''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


1zbx, resolution 2.5Å

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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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