1nyh
From Proteopedia
(New page: 200px<br /><applet load="1nyh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nyh, resolution 3.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:1nyh.jpg|left|200px]]<br /><applet load="1nyh" size=" | + | [[Image:1nyh.jpg|left|200px]]<br /><applet load="1nyh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nyh, resolution 3.10Å" /> | caption="1nyh, resolution 3.10Å" /> | ||
'''Crystal Structure of the Coiled-coil Dimerization Motif of Sir4'''<br /> | '''Crystal Structure of the Coiled-coil Dimerization Motif of Sir4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The yeast silent information regulators Sir2, Sir3, and Sir4 physically | + | The yeast silent information regulators Sir2, Sir3, and Sir4 physically interact with one another to establish a transcriptionally silent state by forming repressive chromatin structures. The Sir4 protein contains binding sites for both Sir2 and Sir3, and these protein-protein interactions are required for gene silencing. Here, we report the X-ray structure of the coiled-coil dimerization motif within the C-terminus of Sir4 and show that it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues 464-978). We have identified a cluster of residues on the surface of the Sir4 coiled coil required for specific interactions with Sir3. The histone deacetylase Sir2 can also bind to this complex, forming a ternary complex with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4 with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to chromatin by virtue of its interactions with Sir4 and with deacetylated histones in chromatin. |
==About this Structure== | ==About this Structure== | ||
| - | 1NYH 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:// | + | 1NYH 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=1NYH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chang, J | + | [[Category: Chang, J F.]] |
[[Category: Ellenberger, T.]] | [[Category: Ellenberger, T.]] | ||
[[Category: Filman, D.]] | [[Category: Filman, D.]] | ||
| - | [[Category: Hall, B | + | [[Category: Hall, B E.]] |
[[Category: Moazed, D.]] | [[Category: Moazed, D.]] | ||
| - | [[Category: Tanny, J | + | [[Category: Tanny, J C.]] |
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
[[Category: repressor]] | [[Category: repressor]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:25 2008'' |
Revision as of 12:11, 21 February 2008
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Crystal Structure of the Coiled-coil Dimerization Motif of Sir4
Overview
The yeast silent information regulators Sir2, Sir3, and Sir4 physically interact with one another to establish a transcriptionally silent state by forming repressive chromatin structures. The Sir4 protein contains binding sites for both Sir2 and Sir3, and these protein-protein interactions are required for gene silencing. Here, we report the X-ray structure of the coiled-coil dimerization motif within the C-terminus of Sir4 and show that it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues 464-978). We have identified a cluster of residues on the surface of the Sir4 coiled coil required for specific interactions with Sir3. The histone deacetylase Sir2 can also bind to this complex, forming a ternary complex with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4 with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to chromatin by virtue of its interactions with Sir4 and with deacetylated histones in chromatin.
About this Structure
1NYH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the coiled-coil dimerization motif of Sir4 and its interaction with Sir3., Chang JF, Hall BE, Tanny JC, Moazed D, Filman D, Ellenberger T, Structure. 2003 Jun;11(6):637-49. PMID:12791253
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