1z1a: Difference between revisions

Revision as of 17:11, 21 February 2008

S. cerevisiae Sir1 ORC-interaction domain

OverviewOverview

The Sir1 protein plays a key role in establishing a silent chromatin structure at the cryptic mating-type loci HMR and HML in Saccharomyces cerevisiae by interacting with the bromo-adjacent homology (BAH) domain of the Orc1p subunit of the origin recognition complex (ORC). Here, we present the high-resolution crystal structures of the ORC interaction region (OIR) of Sir1p and that of the complex formed between the OIR and BAH domains. Amino acids within the OIR previously shown to be required for a Sir1p/ORC interaction are presented on a conserved, convex surface that forms a complementary interface with a concave region of the Orc1 BAH domain that is critical for transcriptional silencing. The OIR/BAH interaction surface comprises a network of hydrophobic and polar/ionic interactions between discrete structural modules in each protein and involves several residues that were not implicated in previous studies. These data provide important structural insights into a protein-protein interaction critical for the formation of a specialized chromatin domain within eukaryotic chromosomes.

About this StructureAbout this Structure

1Z1A is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing., Hou Z, Bernstein DA, Fox CA, Keck JL, Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8489-94. Epub 2005 Jun 2. PMID:15932939

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OCA

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-[[Image:1z1a.gif|left|200px]]<br /><applet load="1z1a" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1z1a.gif|left|200px]]<br /><applet load="1z1a" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1z1a, resolution 2.50&Aring;" />
 '''S. cerevisiae Sir1 ORC-interaction domain'''<br />
 ==Overview==
-The Sir1 protein plays a key role in establishing a silent chromatin, structure at the cryptic mating-type loci HMR and HML in Saccharomyces, cerevisiae by interacting with the bromo-adjacent homology (BAH) domain of, the Orc1p subunit of the origin recognition complex (ORC). Here, we, present the high-resolution crystal structures of the ORC interaction, region (OIR) of Sir1p and that of the complex formed between the OIR and, BAH domains. Amino acids within the OIR previously shown to be required, for a Sir1p/ORC interaction are presented on a conserved, convex surface, that forms a complementary interface with a concave region of the Orc1 BAH, domain that is critical for transcriptional silencing. The OIR/BAH, interaction surface comprises a network of hydrophobic and polar/ionic, interactions between discrete structural modules in each protein and, involves several residues that were not implicated in previous studies., These data provide important structural insights into a protein-protein, interaction critical for the formation of a specialized chromatin domain, within eukaryotic chromosomes.
+The Sir1 protein plays a key role in establishing a silent chromatin structure at the cryptic mating-type loci HMR and HML in Saccharomyces cerevisiae by interacting with the bromo-adjacent homology (BAH) domain of the Orc1p subunit of the origin recognition complex (ORC). Here, we present the high-resolution crystal structures of the ORC interaction region (OIR) of Sir1p and that of the complex formed between the OIR and BAH domains. Amino acids within the OIR previously shown to be required for a Sir1p/ORC interaction are presented on a conserved, convex surface that forms a complementary interface with a concave region of the Orc1 BAH domain that is critical for transcriptional silencing. The OIR/BAH interaction surface comprises a network of hydrophobic and polar/ionic interactions between discrete structural modules in each protein and involves several residues that were not implicated in previous studies. These data provide important structural insights into a protein-protein interaction critical for the formation of a specialized chromatin domain within eukaryotic chromosomes.
 ==About this Structure==
-Z1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1Z1A OCA].
+Z1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1Z1A OCA].
 ==Reference==
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 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Bernstein, D.A.]]
+[[Category: Bernstein, D A.]]
-[[Category: Fox, C.A.]]
+[[Category: Fox, C A.]]
 [[Category: Hou, Z.]]
-[[Category: Keck, J.L.]]
+[[Category: Keck, J L.]]
 [[Category: novel fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:11:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:11 2008''