1m4z

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(New page: 200px<br /><applet load="1m4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4z, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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[[Image:1m4z.jpg|left|200px]]<br /><applet load="1m4z" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m4z.jpg|left|200px]]<br /><applet load="1m4z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m4z, resolution 2.2&Aring;" />
caption="1m4z, resolution 2.2&Aring;" />
'''Crystal structure of the N-terminal BAH domain of Orc1p'''<br />
'''Crystal structure of the N-terminal BAH domain of Orc1p'''<br />
==Overview==
==Overview==
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The N-terminal domain of the largest subunit of the Saccharomyces, cerevisiae origin recognition complex (Orc1p) functions in transcriptional, silencing and contains a bromo-adjacent homology (BAH) domain found in, some chromatin-associated proteins including Sir3p. The 2.2 A crystal, structure of the N-terminal domain of Orc1p revealed a BAH core and a, non-conserved helical sub-domain. Mutational analyses demonstrated that, the helical sub-domain was necessary and sufficient to bind Sir1p, and, critical for targeting Sir1p primarily to the cis-acting E silencers at, the HMR and HML silent chromatin domains. In the absence of the BAH, domain, approximately 14-20% of cells in a population were silenced at the, HML locus. Moreover, the distributions of the Sir2p, Sir3p and Sir4p, proteins, while normal, were at levels lower than found in wild-type, cells. Thus, in the absence of the Orc1p BAH domain, HML resembled, silencing of genes adjacent to telomeres. These data are consistent with, the view that the Orc1p-Sir1p interaction at the E silencers ensures, stable inheritance of pre-established Sir2p, Sir3p and Sir4p complexes at, the silent mating type loci.
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The N-terminal domain of the largest subunit of the Saccharomyces cerevisiae origin recognition complex (Orc1p) functions in transcriptional silencing and contains a bromo-adjacent homology (BAH) domain found in some chromatin-associated proteins including Sir3p. The 2.2 A crystal structure of the N-terminal domain of Orc1p revealed a BAH core and a non-conserved helical sub-domain. Mutational analyses demonstrated that the helical sub-domain was necessary and sufficient to bind Sir1p, and critical for targeting Sir1p primarily to the cis-acting E silencers at the HMR and HML silent chromatin domains. In the absence of the BAH domain, approximately 14-20% of cells in a population were silenced at the HML locus. Moreover, the distributions of the Sir2p, Sir3p and Sir4p proteins, while normal, were at levels lower than found in wild-type cells. Thus, in the absence of the Orc1p BAH domain, HML resembled silencing of genes adjacent to telomeres. These data are consistent with the view that the Orc1p-Sir1p interaction at the E silencers ensures stable inheritance of pre-established Sir2p, Sir3p and Sir4p complexes at the silent mating type loci.
==About this Structure==
==About this Structure==
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1M4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M4Z OCA].
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1M4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4Z OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hayashi, M.K.]]
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[[Category: Hayashi, M K.]]
[[Category: Merkel, O.]]
[[Category: Merkel, O.]]
[[Category: Stillman, B.]]
[[Category: Stillman, B.]]
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[[Category: Xu, R.M.]]
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[[Category: Xu, R M.]]
[[Category: Zhang, Z.]]
[[Category: Zhang, Z.]]
[[Category: MN]]
[[Category: MN]]
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[[Category: transcriptional silencing]]
[[Category: transcriptional silencing]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:09:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:33 2008''

Revision as of 11:51, 21 February 2008


1m4z, resolution 2.2Å

Drag the structure with the mouse to rotate

Crystal structure of the N-terminal BAH domain of Orc1p

Overview

The N-terminal domain of the largest subunit of the Saccharomyces cerevisiae origin recognition complex (Orc1p) functions in transcriptional silencing and contains a bromo-adjacent homology (BAH) domain found in some chromatin-associated proteins including Sir3p. The 2.2 A crystal structure of the N-terminal domain of Orc1p revealed a BAH core and a non-conserved helical sub-domain. Mutational analyses demonstrated that the helical sub-domain was necessary and sufficient to bind Sir1p, and critical for targeting Sir1p primarily to the cis-acting E silencers at the HMR and HML silent chromatin domains. In the absence of the BAH domain, approximately 14-20% of cells in a population were silenced at the HML locus. Moreover, the distributions of the Sir2p, Sir3p and Sir4p proteins, while normal, were at levels lower than found in wild-type cells. Thus, in the absence of the Orc1p BAH domain, HML resembled silencing of genes adjacent to telomeres. These data are consistent with the view that the Orc1p-Sir1p interaction at the E silencers ensures stable inheritance of pre-established Sir2p, Sir3p and Sir4p complexes at the silent mating type loci.

About this Structure

1M4Z is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and function of the BAH-containing domain of Orc1p in epigenetic silencing., Zhang Z, Hayashi MK, Merkel O, Stillman B, Xu RM, EMBO J. 2002 Sep 2;21(17):4600-11. PMID:12198162

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